ID   DEGPL_RHIME             Reviewed;         504 AA.
AC   Q52894;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Probable periplasmic serine endoprotease DegP-like;
DE            EC=3.4.21.107;
DE   AltName: Full=Protease Do;
DE   Flags: Precursor;
GN   Name=degP1; Synonyms=degP; OrderedLocusNames=R01021; ORFNames=SMc02365;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=8550509; DOI=10.1128/jb.178.3.745-752.1996;
RA   Glazebrook J., Ichige A., Walker G.C.;
RT   "Genetic analysis of Rhizobium meliloti bacA-phoA fusion results in
RT   identification of degP: two loci required for symbiosis are closely linked
RT   to degP.";
RL   J. Bacteriol. 178:745-752(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
CC   -!- FUNCTION: Might be efficient in the degradation of transiently
CC       denatured and unfolded proteins which accumulate in the periplasm
CC       following stress conditions. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Acts on substrates that are at least partially unfolded. The
CC         cleavage site P1 residue is normally between a pair of hydrophobic
CC         residues, such as Val-|-Val.; EC=3.4.21.107;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC43669.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U31512; AAC43669.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL591688; CAC45593.1; -; Genomic_DNA.
DR   RefSeq; NP_385127.1; NC_003047.1.
DR   AlphaFoldDB; Q52894; -.
DR   SMR; Q52894; -.
DR   STRING; 266834.SMc02365; -.
DR   EnsemblBacteria; CAC45593; CAC45593; SMc02365.
DR   KEGG; sme:SMc02365; -.
DR   PATRIC; fig|266834.11.peg.2426; -.
DR   eggNOG; COG0265; Bacteria.
DR   HOGENOM; CLU_020120_1_0_5; -.
DR   OMA; RALFQIQ; -.
DR   Proteomes; UP000001976; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISS:UniProtKB.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011782; Pept_S1C_Do.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   Pfam; PF13180; PDZ_2; 2.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; SSF50156; 2.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   TIGRFAMs; TIGR02037; degP_htrA_DO; 1.
DR   PROSITE; PS50106; PDZ; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Periplasm; Protease; Reference proteome; Repeat;
KW   Serine protease; Signal; Stress response.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..504
FT                   /note="Probable periplasmic serine endoprotease DegP-like"
FT                   /id="PRO_0000026933"
FT   DOMAIN          287..378
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          401..491
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          102..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..286
FT                   /note="Serine protease"
FT   REGION          389..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        140
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        170
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        244
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255"
FT   BINDING         242..244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         299..303
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        14..15
FT                   /note="LL -> PV (in Ref. 1; AAC43669)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39..147
FT                   /note="PSFANVVDAVSPAVVSVRVQARERVSDDESNFTFDFGGRGFEDLPEDHPLRR
FT                   FFREFAPRENDRADRWRDRRGPRGEGRLRPRAQGSGFFITEDGYLVTNNHVVSDGSA
FT                   -> AVSPMWSTPFRRRSSPSACRHVNASATMKATSPSISAAAGSRTCRKTIRCGVSSAN
FT                   SLRVKMTVPIVGATAAVRVAKVVSVRGRKAPASSSPKTVTSSPTTTSSPTART (in
FT                   Ref. 1; AAC43669)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464..504
FT                   /note="KSADDVLKVINNAKKDGRSKALFQIEAQEGSRFVALPITQG -> NRQTTFS
FT                   R (in Ref. 1; AAC43669)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   504 AA;  53035 MW;  D7E82BB9981EA23C CRC64;
     MLKTTTVAGL AAVLLTTGLP AEVAQSFAEA VRVQAPAVPS FANVVDAVSP AVVSVRVQAR
     ERVSDDESNF TFDFGGRGFE DLPEDHPLRR FFREFAPREN DRADRWRDRR GPRGEGRLRP
     RAQGSGFFIT EDGYLVTNNH VVSDGSAFTV IMNDGTELDA KLVGKDSRTD LAVLKVDDKR
     KFTYVSFADD EKVRVGDWVV AVGNPFGLGG TVTAGIISAR GRDIGSGPYD DYLQVDAAVN
     RGNSGGPTFN LSGEVVGINT AIFSPSGGNV GIAFAIPASV AKDVVDSLIK DGTVSRGWLG
     VQIQPVTKDI AESLGLSEAN GALVVEPQAG SPGEKAGIKN GDVVTALNGE PVKDPRDLAR
     RVAALRPGST AEVTLWRSGK SETVNLEIGT LPSDAKEPAP ATGEAQPDEG QAGEEALADL
     GLTVTPSEDG KGVTIASVDP DSDAGDRGLK EGEKIVSVNN QEVKSADDVL KVINNAKKDG
     RSKALFQIEA QEGSRFVALP ITQG