CLPA_ECOLI
ID CLPA_ECOLI Reviewed; 758 AA.
AC P0ABH9; P15716; P77686;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA;
GN Name=clpA; Synonyms=lopD; OrderedLocusNames=b0882, JW0866;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2186030; DOI=10.1016/s0021-9258(19)39014-3;
RA Gottesman S., Clark W.P., Maurizi M.R.;
RT "The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and
RT identification of a Clp-specific substrate.";
RL J. Biol. Chem. 265:7886-7893(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=SG1110;
RX PubMed=3049606; DOI=10.1016/s0021-9258(18)68168-2;
RA Katayama Y., Gottesman S., Pumphrey J., Rudikoff S., Clark W.P.,
RA Maurizi M.R.;
RT "The two-component, ATP-dependent Clp protease of Escherichia coli.
RT Purification, cloning, and mutational analysis of the ATP-binding
RT component.";
RL J. Biol. Chem. 263:15226-15236(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 511-758.
RX PubMed=1909328; DOI=10.1016/s0021-9258(18)55327-8;
RA Cummings H.S., Sands J.F., Foreman P.C., Fraser J., Hershey J.W.B.;
RT "Structure and expression of the infA operon encoding translational
RT initiation factor IF1. Transcriptional control by growth rate.";
RL J. Biol. Chem. 266:16491-16498(1991).
RN [7]
RP SIMILARITY TO OTHER CLPAB LIKE PROTEINS.
RX PubMed=2185473; DOI=10.1073/pnas.87.9.3513;
RA Gottesman S., Squires C., Pichersky E., Carrington M., Hobbs M.,
RA Mattick J.S., Dalrymple B., Kuramitsu H., Shiroza T., Foster T.,
RA Clark W.P., Ross B., Squires C.L., Maurizi M.R.;
RT "Conservation of the regulatory subunit for the Clp ATP-dependent protease
RT in prokaryotes and eukaryotes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3513-3517(1990).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-143.
RX PubMed=12205096; DOI=10.1074/jbc.m207796200;
RA Guo F., Maurizi M.R., Esser L., Xia D.;
RT "Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP
RT protease.";
RL J. Biol. Chem. 277:46743-46752(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-146 IN COMPLEX WITH CLPS.
RX PubMed=12426582; DOI=10.1038/nsb869;
RA Zeth K., Ravelli R.B., Paal K., Cusack S., Bukau B., Dougan D.A.;
RT "Structural analysis of the adaptor protein ClpS in complex with the N-
RT terminal domain of ClpA.";
RL Nat. Struct. Biol. 9:906-911(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-143 IN COMPLEX WITH CLPS.
RX PubMed=12235156; DOI=10.1074/jbc.m208104200;
RA Guo F., Esser L., Singh S.K., Maurizi M.R., Xia D.;
RT "Crystal structure of the heterodimeric complex of the adaptor, ClpS, with
RT the N-domain of the AAA+ chaperone, ClpA.";
RL J. Biol. Chem. 277:46753-46762(2002).
CC -!- FUNCTION: ATP-dependent specificity component of the ClpAP protease. It
CC directs the protease to specific substrates. It has unfoldase activity.
CC The primary function of the ClpA-ClpP complex appears to be the
CC degradation of unfolded or abnormal proteins.
CC -!- SUBUNIT: Component of the ClpAP complex composed of six ClpA subunits
CC assembled into a hexameric ring in the presence of ATP, and fourteen
CC ClpP subunits arranged in two heptameric rings. Binds to ClpS.
CC {ECO:0000269|PubMed:12235156, ECO:0000269|PubMed:12426582}.
CC -!- INTERACTION:
CC P0ABH9; P0AEC5: barA; NbExp=3; IntAct=EBI-546140, EBI-546740;
CC P0ABH9; P0A6G7: clpP; NbExp=11; IntAct=EBI-546140, EBI-370625;
CC P0ABH9; P0A8Q6: clpS; NbExp=13; IntAct=EBI-546140, EBI-561456;
CC P0ABH9; P68646: fixX; NbExp=2; IntAct=EBI-546140, EBI-1113234;
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; M31045; AAA23583.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73969.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35601.1; -; Genomic_DNA.
DR EMBL; M23220; AAA23582.1; -; Genomic_DNA.
DR PIR; B64827; SUECCA.
DR RefSeq; NP_415403.1; NC_000913.3.
DR RefSeq; WP_000934041.1; NZ_STEB01000006.1.
DR PDB; 1K6K; X-ray; 1.80 A; A=1-143.
DR PDB; 1KSF; X-ray; 2.60 A; X=1-758.
DR PDB; 1LZW; X-ray; 2.50 A; B=1-146.
DR PDB; 1MBU; X-ray; 2.30 A; A/B=1-142.
DR PDB; 1MBV; X-ray; 3.30 A; A=1-142.
DR PDB; 1MBX; X-ray; 2.25 A; A/B=1-142.
DR PDB; 1MG9; X-ray; 2.30 A; B=1-146.
DR PDB; 1R6B; X-ray; 2.25 A; X=1-758.
DR PDB; 1R6C; X-ray; 2.15 A; X=1-143.
DR PDB; 1R6O; X-ray; 2.25 A; A/B=1-143.
DR PDB; 1R6Q; X-ray; 2.35 A; A/B=1-143.
DR PDB; 5OFO; EM; 4.60 A; A/B/C/D/E/F=609-635.
DR PDB; 5OG1; EM; 4.50 A; A/B/C/D/E/F=609-635.
DR PDB; 6UQE; EM; 3.00 A; A/B/C/D/E/F=169-746.
DR PDB; 6UQO; EM; 3.10 A; A/B/C/D/E/F=169-746.
DR PDB; 6W1Z; EM; 2.70 A; A/B/C/D/E/F=1-758.
DR PDB; 6W20; EM; 3.00 A; A/B/C/D/E/F=1-758.
DR PDB; 6W21; EM; 3.30 A; A/B/C/D/E/F=1-758.
DR PDB; 6W22; EM; 3.00 A; A/B/C/D/E/F=1-758.
DR PDB; 6W23; EM; 3.10 A; A/B/C/D/E/F=1-758.
DR PDB; 6W24; EM; 3.40 A; A/B/C/D/E/F=1-758.
DR PDBsum; 1K6K; -.
DR PDBsum; 1KSF; -.
DR PDBsum; 1LZW; -.
DR PDBsum; 1MBU; -.
DR PDBsum; 1MBV; -.
DR PDBsum; 1MBX; -.
DR PDBsum; 1MG9; -.
DR PDBsum; 1R6B; -.
DR PDBsum; 1R6C; -.
DR PDBsum; 1R6O; -.
DR PDBsum; 1R6Q; -.
DR PDBsum; 5OFO; -.
DR PDBsum; 5OG1; -.
DR PDBsum; 6UQE; -.
DR PDBsum; 6UQO; -.
DR PDBsum; 6W1Z; -.
DR PDBsum; 6W20; -.
DR PDBsum; 6W21; -.
DR PDBsum; 6W22; -.
DR PDBsum; 6W23; -.
DR PDBsum; 6W24; -.
DR AlphaFoldDB; P0ABH9; -.
DR SMR; P0ABH9; -.
DR BioGRID; 4261320; 452.
DR BioGRID; 850131; 5.
DR ComplexPortal; CPX-3175; Endopeptidase ClpAP complex.
DR DIP; DIP-35409N; -.
DR IntAct; P0ABH9; 77.
DR MINT; P0ABH9; -.
DR STRING; 511145.b0882; -.
DR MEROPS; X20.001; -.
DR jPOST; P0ABH9; -.
DR PaxDb; P0ABH9; -.
DR PRIDE; P0ABH9; -.
DR EnsemblBacteria; AAC73969; AAC73969; b0882.
DR EnsemblBacteria; BAA35601; BAA35601; BAA35601.
DR GeneID; 66670844; -.
DR GeneID; 945764; -.
DR KEGG; ecj:JW0866; -.
DR KEGG; eco:b0882; -.
DR PATRIC; fig|1411691.4.peg.1395; -.
DR EchoBASE; EB0154; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_6; -.
DR InParanoid; P0ABH9; -.
DR OMA; GRVIQEH; -.
DR PhylomeDB; P0ABH9; -.
DR BioCyc; EcoCyc:EG10156-MON; -.
DR BioCyc; MetaCyc:EG10156-MON; -.
DR SABIO-RK; P0ABH9; -.
DR EvolutionaryTrace; P0ABH9; -.
DR PRO; PR:P0ABH9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009368; C:endopeptidase Clp complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IDA:EcoCyc.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IDA:CACAO.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IC:ComplexPortal.
DR GO; GO:0043335; P:protein unfolding; IMP:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR013461; ClpA.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR TIGRFAMs; TIGR02639; ClpA; 1.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chaperone; Direct protein sequencing;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..758
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpA"
FT /id="PRO_0000191079"
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 2..65
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 80..145
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 140..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..417
FT /note="I"
FT REGION 421..609
FT /note="II"
FT COMPBIAS 142..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 214..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 495..502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 367
FT /note="A -> G (in Ref. 1; AAA23583)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="L -> V (in Ref. 1; AAA23583)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="L -> V (in Ref. 1; AAA23583)"
FT /evidence="ECO:0000305"
FT HELIX 4..20
FT /evidence="ECO:0007829|PDB:1K6K"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1K6K"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:1K6K"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:1K6K"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:1K6K"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 82..96
FT /evidence="ECO:0007829|PDB:1K6K"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1K6K"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 105..112
FT /evidence="ECO:0007829|PDB:1K6K"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:1K6K"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:1K6K"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6UQE"
FT HELIX 192..202
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 220..233
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:6W1Z"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:1KSF"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:1R6B"
FT TURN 285..292
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 300..307
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 324..328
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 329..333
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:6UQO"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 351..369
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 375..388
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 396..411
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:6W1Z"
FT HELIX 423..433
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 445..456
FT /evidence="ECO:0007829|PDB:1R6B"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 464..478
FT /evidence="ECO:0007829|PDB:1R6B"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:6W20"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:1KSF"
FT STRAND 488..494
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 497..500
FT /evidence="ECO:0007829|PDB:6UQO"
FT HELIX 501..512
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 521..523
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 525..528
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 541..545
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 548..555
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 557..564
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 571..583
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:1R6B"
FT TURN 589..591
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 592..595
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 599..605
FT /evidence="ECO:0007829|PDB:1R6B"
FT TURN 607..609
FT /evidence="ECO:0007829|PDB:6W1Z"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:6W1Z"
FT STRAND 617..620
FT /evidence="ECO:0007829|PDB:6W1Z"
FT HELIX 629..635
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 638..641
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 645..649
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 655..675
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 678..682
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 684..694
FT /evidence="ECO:0007829|PDB:1R6B"
FT TURN 697..699
FT /evidence="ECO:0007829|PDB:1R6B"
FT TURN 701..703
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 704..712
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 714..716
FT /evidence="ECO:0007829|PDB:1R6B"
FT HELIX 717..722
FT /evidence="ECO:0007829|PDB:1R6B"
FT TURN 724..727
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 729..736
FT /evidence="ECO:0007829|PDB:1R6B"
FT TURN 737..740
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 741..748
FT /evidence="ECO:0007829|PDB:1R6B"
FT STRAND 750..752
FT /evidence="ECO:0007829|PDB:1KSF"
SQ SEQUENCE 758 AA; 84207 MW; 0C96A2EB64A9F7DC CRC64;
MLNQELELSL NMAFARAREH RHEFMTVEHL LLALLSNPSA REALEACSVD LVALRQELEA
FIEQTTPVLP ASEEERDTQP TLSFQRVLQR AVFHVQSSGR NEVTGANVLV AIFSEQESQA
AYLLRKHEVS RLDVVNFISH GTRKDEPTQS SDPGSQPNSE EQAGGEERME NFTTNLNQLA
RVGGIDPLIG REKELERAIQ VLCRRRKNNP LLVGESGVGK TAIAEGLAWR IVQGDVPEVM
ADCTIYSLDI GSLLAGTKYR GDFEKRFKAL LKQLEQDTNS ILFIDEIHTI IGAGAASGGQ
VDAANLIKPL LSSGKIRVIG STTYQEFSNI FEKDRALARR FQKIDITEPS IEETVQIING
LKPKYEAHHD VRYTAKAVRA AVELAVKYIN DRHLPDKAID VIDEAGARAR LMPVSKRKKT
VNVADIESVV ARIARIPEKS VSQSDRDTLK NLGDRLKMLV FGQDKAIEAL TEAIKMARAG
LGHEHKPVGS FLFAGPTGVG KTEVTVQLSK ALGIELLRFD MSEYMERHTV SRLIGAPPGY
VGFDQGGLLT DAVIKHPHAV LLLDEIEKAH PDVFNILLQV MDNGTLTDNN GRKADFRNVV
LVMTTNAGVR ETERKSIGLI HQDNSTDAME EIKKIFTPEF RNRLDNIIWF DHLSTDVIHQ
VVDKFIVELQ VQLDQKGVSL EVSQEARNWL AEKGYDRAMG ARPMARVIQD NLKKPLANEL
LFGSLVDGGQ VTVALDKEKN ELTYGFQSAQ KHKAEAAH
