PEPB_YERPE
ID PEPB_YERPE Reviewed; 432 AA.
AC P58475; Q0WD15;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Peptidase B {ECO:0000255|HAMAP-Rule:MF_00504};
DE EC=3.4.11.23 {ECO:0000255|HAMAP-Rule:MF_00504};
DE AltName: Full=Aminopeptidase B {ECO:0000255|HAMAP-Rule:MF_00504};
GN Name=pepB {ECO:0000255|HAMAP-Rule:MF_00504};
GN OrderedLocusNames=YPO2889, y1342, YP_2566;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
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).
CC -!- FUNCTION: Probably plays an important role in intracellular peptide
CC degradation. {ECO:0000255|HAMAP-Rule:MF_00504}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa, from a peptide or
CC arylamide. Xaa is preferably Glu or Asp but may be other amino acids,
CC including Leu, Met, His, Cys and Gln.; EC=3.4.11.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00504};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00504};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00504};
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00504}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00504}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000255|HAMAP-
CC Rule:MF_00504}.
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DR EMBL; AL590842; CAL21500.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84915.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62762.1; -; Genomic_DNA.
DR PIR; AI0351; AI0351.
DR RefSeq; WP_002209829.1; NZ_WUCM01000090.1.
DR RefSeq; YP_002347823.1; NC_003143.1.
DR PDB; 6CXD; X-ray; 2.75 A; A=1-432.
DR PDBsum; 6CXD; -.
DR AlphaFoldDB; P58475; -.
DR SMR; P58475; -.
DR IntAct; P58475; 2.
DR STRING; 214092.YPO2889; -.
DR MEROPS; M17.004; -.
DR PaxDb; P58475; -.
DR DNASU; 1146289; -.
DR EnsemblBacteria; AAM84915; AAM84915; y1342.
DR EnsemblBacteria; AAS62762; AAS62762; YP_2566.
DR GeneID; 57975846; -.
DR KEGG; ype:YPO2889; -.
DR KEGG; ypk:y1342; -.
DR KEGG; ypm:YP_2566; -.
DR PATRIC; fig|214092.21.peg.3339; -.
DR eggNOG; COG0260; Bacteria.
DR HOGENOM; CLU_013734_7_1_6; -.
DR OMA; EKSWAFW; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IBA:GO_Central.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00433; Peptidase_M17; 1.
DR HAMAP; MF_00504; Aminopeptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR008330; Pept_M17_PepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF12404; DUF3663; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PIRSF; PIRSF036388; Ctsl_amnpptdse_B; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cytoplasm; Hydrolase; Manganese;
KW Metal-binding; Protease; Reference proteome.
FT CHAIN 1..432
FT /note="Peptidase B"
FT /id="PRO_0000165851"
FT ACT_SITE 208
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT ACT_SITE 282
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 219
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 278
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 280
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 280
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 95..116
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 124..138
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:6CXD"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 189..201
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 215..218
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 221..235
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 240..251
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 281..293
FT /evidence="ECO:0007829|PDB:6CXD"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 326..338
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 350..354
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:6CXD"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 375..383
FT /evidence="ECO:0007829|PDB:6CXD"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 391..397
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:6CXD"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:6CXD"
FT HELIX 419..429
FT /evidence="ECO:0007829|PDB:6CXD"
SQ SEQUENCE 432 AA; 46531 MW; 57FDBB6B4DB67F2D CRC64;
MTTEIMQISL SHNPADARWG EKALISTNDQ GVTIHLTSHD QLGGIQRAAR KIDGQGIKQV
KLAGEGWGLE QSWAFWQGFR GPKGQRSVVW AELPANEKTE LEQRLKIIDW VRDTINAPAE
DLGPEQLAKN AIDLLCAVSC DAVSYRITKG EDLREQNYAG IYTVGRGSDR APVLLALDYN
PTGNPDAPVM ACLVGKGITF DSGGYSLKQS AFMDSMKSDM GGAATLTGAL ALAAARGLKE
RVKLYLCCAD NMVSGNAFKL GDIIRYRNGK TVEIMNTDAE GRLVLADGLI DASEQNAPLI
IDAATLTGAA KTALGNDYHA LFSFDDELAQ ALLNSAHSEH ELFWRLPLAE FHRSQLPSNF
AELNNVAGGA YSAGASTAAA FLSHFVKNYQ QGWLHIDCSA TYRKSAVDQW SAGATGLGVR
TVANLLLAQA KQ
