PEPB_SALTY
ID PEPB_SALTY Reviewed; 427 AA.
AC Q9RF52;
DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Peptidase B;
DE EC=3.4.11.23;
DE AltName: Full=Aminopeptidase B;
GN Name=pepB; OrderedLocusNames=STM2536;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE,
RP CHARACTERIZATION, AND MUTAGENESIS OF LYS-310.
RC STRAIN=LT2, and TN5179;
RX PubMed=10852868; DOI=10.1128/jb.182.12.3383-3393.2000;
RA Mathew Z., Knox T.M., Miller C.G.;
RT "Salmonella enterica serovar typhimurium peptidase B is a leucyl
RT aminopeptidase with specificity for acidic amino acids.";
RL J. Bacteriol. 182:3383-3393(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Probably plays an important role in intracellular peptide
CC degradation.
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 2 manganese ions per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5-9.5.;
CC -!- SUBUNIT: Homohexamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
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DR EMBL; AF201078; AAF19377.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21430.1; -; Genomic_DNA.
DR RefSeq; NP_461471.1; NC_003197.2.
DR RefSeq; WP_000133541.1; NC_003197.2.
DR AlphaFoldDB; Q9RF52; -.
DR SMR; Q9RF52; -.
DR STRING; 99287.STM2536; -.
DR MEROPS; M17.004; -.
DR PaxDb; Q9RF52; -.
DR EnsemblBacteria; AAL21430; AAL21430; STM2536.
DR GeneID; 1254058; -.
DR KEGG; stm:STM2536; -.
DR PATRIC; fig|99287.12.peg.2676; -.
DR HOGENOM; CLU_013734_7_1_6; -.
DR OMA; EKSWAFW; -.
DR PhylomeDB; Q9RF52; -.
DR BioCyc; SENT99287:STM2536-MON; -.
DR BRENDA; 3.4.11.1; 2169.
DR Proteomes; UP000001014; 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 Aminopeptidase; Cytoplasm; Direct protein sequencing; Hydrolase; Manganese;
KW Metal-binding; Protease; Reference proteome.
FT CHAIN 1..427
FT /note="Peptidase B"
FT /id="PRO_0000165842"
FT ACT_SITE 207
FT /evidence="ECO:0000255"
FT ACT_SITE 281
FT /evidence="ECO:0000255"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MUTAGEN 310
FT /note="K->V: Reduces the ability to hydrolyze Asp-Leu
FT without decreasing its ability to hydrolyze Leu-Leu."
FT /evidence="ECO:0000269|PubMed:10852868"
SQ SEQUENCE 427 AA; 46355 MW; 37CCAE4C8771F499 CRC64;
MTEAMKITLS TQPADARWGD KATYSINNDG ITLHLNGKDD LGLIQRAARK IDGLGIKQVA
LTGEGWDTER CWAFWAGYKG PKGVRTVMWP DLDDAQRQEL DNRLTIIDWV RDTINAPAEE
LGPEQLAQRA VDLLCSVACD SVTYRITKGE DLREQNYMGL HTVGRGSERP PVLLALDYNP
TGDKDAPVYA CLVGKGITFD SGGYSIKQSA FMDSMKSDMG GAATVTGALA FAITRGLNKR
VKLFLCCADN LISGNAFKLG DIIRYRNGKN VEVMNTDAEG RLVLADGLID ASAQHPQLII
DMATLTGAAK TALGNDYHAL FSFDDTLAGR LLTSAAQENE PFWRLPLAEF HRNQLPSNFA
ELNNTGSAAY PAGASTAAGF LSHFVENYRE GWLHIDCSAT YRKAPVEQWA AGATGLGVRT
IANLLTA
