YOPM_YERPE
ID YOPM_YERPE Reviewed; 409 AA.
AC P17778; O68701;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Outer membrane protein YopM;
GN Name=yopM; Synonyms=yop48;
GN OrderedLocusNames=YPCD1.26c, y5054, y0059, YP_pCD60;
OS Yersinia pestis.
OG Plasmid pCD1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=2670888; DOI=10.1128/jb.171.9.4623-4632.1989;
RA Leung K.Y., Straley S.C.;
RT "The yopM gene of Yersinia pestis encodes a released protein having
RT homology with the human platelet surface protein GPIb alpha.";
RL J. Bacteriol. 171:4623-4632(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=9746557; DOI=10.1128/iai.66.10.4611-4623.1998;
RA Perry R.D., Straley S.C., Fetherston J.D., Rose D.J., Gregor J.,
RA Blattner F.R.;
RT "DNA sequencing and analysis of the low-Ca2+-response plasmid pCD1 of
RT Yersinia pestis KIM5.";
RL Infect. Immun. 66:4611-4623(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KIM5 / Biovar Mediaevalis;
RX PubMed=9748454; DOI=10.1128/jb.180.19.5192-5202.1998;
RA Hu P., Elliott J., McCready P., Skowronski E., Garnes J., Kobayashi A.,
RA Brubaker R.R., Garcia E.;
RT "Structural organization of virulence-associated plasmids of Yersinia
RT pestis.";
RL J. Bacteriol. 180:5192-5202(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-386, AND DOMAINS LEUCINE-RICH
RP REPEATS.
RX PubMed=11575934; DOI=10.1006/jmbi.2001.4973;
RA Evdokimov A.G., Anderson D.E., Routzahn K.M., Waugh D.S.;
RT "Unusual molecular architecture of the Yersinia pestis cytotoxin YopM: a
RT leucine-rich repeat protein with the shortest repeating unit.";
RL J. Mol. Biol. 312:807-821(2001).
CC -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC promote bacterial survival in host tissues. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer forming a hollow cylinder with an inner diameter
CC of approximately 35 angstroms.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane. Secreted.
CC -!- SIMILARITY: Belongs to the LRR-containing bacterial E3 ligase family.
CC {ECO:0000305}.
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DR EMBL; AF074612; AAC69806.1; -; Genomic_DNA.
DR EMBL; AF053946; AAC62580.1; -; Genomic_DNA.
DR EMBL; AL117189; CAB54903.1; -; Genomic_DNA.
DR EMBL; AE017043; AAS58577.1; -; Genomic_DNA.
DR PIR; A33950; A33950.
DR PIR; T43599; T43599.
DR RefSeq; NP_395161.1; NC_003131.1.
DR RefSeq; NP_857756.1; NC_004836.1.
DR RefSeq; NP_857953.1; NC_004839.1.
DR RefSeq; WP_002229779.1; NC_004839.1.
DR PDB; 1G9U; X-ray; 2.35 A; A=1-409.
DR PDB; 1JL5; X-ray; 2.10 A; A=1-409.
DR PDBsum; 1G9U; -.
DR PDBsum; 1JL5; -.
DR AlphaFoldDB; P17778; -.
DR SMR; P17778; -.
DR IntAct; P17778; 36.
DR STRING; 214092.5832447; -.
DR DNASU; 1149317; -.
DR EnsemblBacteria; AAS58577; AAS58577; YP_pCD60.
DR KEGG; ype:YPCD1.26c; -.
DR KEGG; ypm:YP_pCD60; -.
DR PATRIC; fig|214092.21.peg.33; -.
DR eggNOG; COG4886; Bacteria.
DR HOGENOM; CLU_637685_0_0_6; -.
DR EvolutionaryTrace; P17778; -.
DR PHI-base; PHI:6101; -.
DR PHI-base; PHI:6824; -.
DR PHI-base; PHI:6830; -.
DR Proteomes; UP000000815; Plasmid pCD1.
DR Proteomes; UP000001019; Plasmid pCD1.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR DisProt; DP01639; -.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR032674; LRR_E3_ligase_N.
DR Pfam; PF12468; TTSSLRR; 1.
DR PROSITE; PS51450; LRR; 11.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell outer membrane; Leucine-rich repeat; Membrane;
KW Metal-binding; Plasmid; Reference proteome; Repeat; Secreted.
FT CHAIN 1..409
FT /note="Outer membrane protein YopM"
FT /id="PRO_0000066369"
FT REPEAT 72..91
FT /note="LRR 1"
FT REPEAT 92..113
FT /note="LRR 2"
FT REPEAT 114..131
FT /note="LRR 3"
FT REPEAT 132..153
FT /note="LRR 4"
FT REPEAT 154..173
FT /note="LRR 5"
FT REPEAT 174..195
FT /note="LRR 6"
FT REPEAT 196..215
FT /note="LRR 7"
FT REPEAT 216..237
FT /note="LRR 8"
FT REPEAT 238..257
FT /note="LRR 9"
FT REPEAT 258..279
FT /note="LRR 10"
FT REPEAT 280..297
FT /note="LRR 11"
FT REPEAT 298..317
FT /note="LRR 12"
FT REPEAT 318..339
FT /note="LRR 13"
FT REPEAT 340..357
FT /note="LRR 14"
FT REPEAT 358..379
FT /note="LRR 15"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 307
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT CONFLICT 142..183
FT /note="Missing (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 195..236
FT /note="Missing (in Ref. 5; AAS58577)"
FT /evidence="ECO:0000305"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1G9U"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1JL5"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1G9U"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:1JL5"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:1JL5"
SQ SEQUENCE 409 AA; 46203 MW; E22400C671A59951 CRC64;
MFINPRNVSN TFLQEPLRHS SNLTEMPVEA ENVKSKTEYY NAWSEWERNA PPGNGEQREM
AVSRLRDCLD RQAHELELNN LGLSSLPELP PHLESLVASC NSLTELPELP QSLKSLLVDN
NNLKALSDLP PLLEYLGVSN NQLEKLPELQ NSSFLKIIDV DNNSLKKLPD LPPSLEFIAA
GNNQLEELPE LQNLPFLTAI YADNNSLKKL PDLPLSLESI VAGNNILEEL PELQNLPFLT
TIYADNNLLK TLPDLPPSLE ALNVRDNYLT DLPELPQSLT FLDVSENIFS GLSELPPNLY
YLNASSNEIR SLCDLPPSLE ELNVSNNKLI ELPALPPRLE RLIASFNHLA EVPELPQNLK
QLHVEYNPLR EFPDIPESVE DLRMNSERVV DPYEFAHETT DKLEDDVFE
