PEPB_SHIDS
ID PEPB_SHIDS Reviewed; 427 AA.
AC Q32D41;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 84.
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}; OrderedLocusNames=SDY_2719;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABB62764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000034; ABB62764.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000133554.1; NC_007606.1.
DR RefSeq; YP_404255.2; NC_007606.1.
DR AlphaFoldDB; Q32D41; -.
DR SMR; Q32D41; -.
DR STRING; 300267.SDY_2719; -.
DR MEROPS; M17.004; -.
DR EnsemblBacteria; ABB62764; ABB62764; SDY_2719.
DR KEGG; sdy:SDY_2719; -.
DR PATRIC; fig|300267.13.peg.3280; -.
DR HOGENOM; CLU_013734_7_1_6; -.
DR Proteomes; UP000002716; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease;
KW Reference proteome.
FT CHAIN 1..427
FT /note="Peptidase B"
FT /id="PRO_0000165844"
FT ACT_SITE 207
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT ACT_SITE 281
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 218
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00504"
SQ SEQUENCE 427 AA; 46250 MW; 2F9DAD4A0C08D85F CRC64;
MTEAMKITLS TQPADARWGE KATYSINNDG IILHLNGADD LGLIQRAARK IDGLGIKHVQ
LSGESWDADR CWAFWQGYKA PKGTRKVEWP DLDDAQRQEL DNRLMIIDWV RDTINAPAEE
LGPSQLAQRA VDLISNVAGD RVTYRITKGE DLREQGYMGL HTVGRGSERS PVLLALDYNP
TGDKEAPVYA CLVGKGITFD SGGYSIKQTA FMDSMKSDMG GAATVTGALA FAITRGLNKR
VKLFLCCADN LISGNAFKLG DIITYRNGKK VEVMNTDAEG RLVLADGLID ASAQKPELII
DAATLTGAAK TALGNDYHAL FSFDDALAGR LLASASQENE PFWRLPLAEF HRSQLPSNFA
ELNNTGSAAY PAGASTAAGF LSHFVENYQQ GWLHIDCSAT YRKAPVEQWS AGATGLGVRT
IANLLTA
