ID W1JB96_9GAMM Unreviewed; 441 AA.
AC W1JB96;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Peptidase B {ECO:0000313|EMBL:CDL86785.1};
DE EC=3.4.11.23 {ECO:0000313|EMBL:CDL86785.1};
GN Name=pepB {ECO:0000313|EMBL:CDL86785.1};
GN ORFNames=XCR1_60032 {ECO:0000313|EMBL:CDL86785.1};
OS Xenorhabdus cabanillasii JM26.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427517 {ECO:0000313|EMBL:CDL86785.1, ECO:0000313|Proteomes:UP000019197};
RN [1] {ECO:0000313|EMBL:CDL86785.1, ECO:0000313|Proteomes:UP000019197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JM26 {ECO:0000313|EMBL:CDL86785.1,
RC ECO:0000313|Proteomes:UP000019197};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacterium,
RT Xenorhabdus cabanillasi strain JM26.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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:CDL86785.1}.
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DR EMBL; CBXE010000453; CDL86785.1; -; Genomic_DNA.
DR RefSeq; WP_038267877.1; NZ_NJGH01000006.1.
DR AlphaFoldDB; W1JB96; -.
DR MEROPS; M17.004; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000019197; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 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,
KW ECO:0000313|EMBL:CDL86785.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDL86785.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 286..293
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 441 AA; 47551 MW; B5FC038249666937 CRC64;
MTKHAIPAQI MPITLSYEPA KACWGEKALI SSNDQGITIH LSDSQSDISS KLAVIQRAGR
KINGQGISNV ALAGDGWDLE KSWAFWQGFR APKGLRTIEW PQLSAVEKQE LEHRIKFIDW
VRDTTNIPAE ELGPEQLAQR VIDLFNDVAG TAISYRIIKG DALHEQGYVG VHTVGRGSCR
VPVFLELDFN PSTDKNQPVF ACLVGKGITF DSGGYSLKPS NSMDSMKSDM GGSALLSGAL
ALAIGRGLKQ RVKLFLCIAD NLVSGNAFKL GDIIRYRNGK SVEVMNTDAE GRLVLADGLI
DASAENAPLI IDAATLTGAA KIAVGNDYHS VLSFDDQLAA DLLAAADAEH EQFWRLPLAE
FHRNQLPSSF ADLNNIASPS HSAGASTAAA FLSHFVENYK KGWVHIDCSA TYRKSAVEQW
SAGATGCGVR TIANLLLTKA K
//
