ID A0A085G710_9ENTR Unreviewed; 428 AA.
AC A0A085G710;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Peptidase B {ECO:0000256|HAMAP-Rule:MF_00504};
DE EC=3.4.11.23 {ECO:0000256|HAMAP-Rule:MF_00504};
DE AltName: Full=Aminopeptidase B {ECO:0000256|HAMAP-Rule:MF_00504};
GN Name=pepB {ECO:0000256|HAMAP-Rule:MF_00504,
GN ECO:0000313|EMBL:KFC79505.1};
GN ORFNames=GBAG_3080 {ECO:0000313|EMBL:KFC79505.1};
OS Buttiauxella agrestis ATCC 33320.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Buttiauxella.
OX NCBI_TaxID=1006004 {ECO:0000313|EMBL:KFC79505.1, ECO:0000313|Proteomes:UP000028653};
RN [1] {ECO:0000313|EMBL:KFC79505.1, ECO:0000313|Proteomes:UP000028653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33320 {ECO:0000313|EMBL:KFC79505.1,
RC ECO:0000313|Proteomes:UP000028653};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probably plays an important role in intracellular peptide
CC degradation. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00504};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00504};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00504};
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00504}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00504}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528, ECO:0000256|HAMAP-Rule:MF_00504}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFC79505.1}.
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DR EMBL; JMPI01000051; KFC79505.1; -; Genomic_DNA.
DR RefSeq; WP_034497709.1; NZ_JMPI01000051.1.
DR AlphaFoldDB; A0A085G710; -.
DR STRING; 1006004.GBAG_3080; -.
DR eggNOG; COG0260; Bacteria.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000028653; Unassembled WGS sequence.
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:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00504; Aminopeptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR047620; M17_PepB-like_N.
DR InterPro; IPR008330; Pept_M17_PepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR PANTHER; PTHR11963:SF20; PEPTIDASE B; 1.
DR Pfam; PF12404; DUF3663; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PIRSF; PIRSF036388; Ctsl_amnpptdse_B; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW Rule:MF_00504};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00504};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00504};
KW Manganese {ECO:0000256|HAMAP-Rule:MF_00504};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00504};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00504};
KW Reference proteome {ECO:0000313|Proteomes:UP000028653}.
FT DOMAIN 275..282
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
FT ACT_SITE 207
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT ACT_SITE 281
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 218
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 277
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
FT BINDING 279
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00504"
SQ SEQUENCE 428 AA; 46481 MW; CDDF16F5864B36EF CRC64;
MSEAMKITLS TASADARWGE KAAYSINDEG ITLHLTGKDD LGLIQRAARK IDGQGLKHVQ
LAGEGWDVEK SWAFWQGYRA PKGTRKVDWA VLSDEEQKEL NNRLKIIDWV RHTINTPAEE
LGPEQLASRA VDLLCDVACD NVSYRITKGE DLREQNYMGI HTVGRGSERP PVLLALDYNP
TGNPDAPVYA CLVGKGITFD SGGYSMKQSA FMDSMKSDMG GAATITGALA FAITRGLNKR
VKLFLCCADN LVSGNAFKLG DIIKYRNGKT VEVMNTDAEG RLVLADGLID ASAQKPELII
DCATLTGAAK TALGNDYHAL FSFDDGLVNR LMESAAEENE PFWRLPLAEF HRNQLPSNFA
ELNNTSNASF PAGASTAAGF LSHFVENYHA GWLHIDCSAT YRKGAVEQWS AGATGIGVRA
IANLLVSQ
//
