ID A0A0F5VHL7_9GAMM Unreviewed; 425 AA.
AC A0A0F5VHL7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Aminopeptidase B {ECO:0000313|EMBL:KKD01538.1};
DE EC=3.4.11.23 {ECO:0000313|EMBL:KKD01538.1};
GN ORFNames=KY46_01585 {ECO:0000313|EMBL:KKD01538.1};
OS Photobacterium halotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=265726 {ECO:0000313|EMBL:KKD01538.1, ECO:0000313|Proteomes:UP000033633};
RN [1] {ECO:0000313|EMBL:KKD01538.1, ECO:0000313|Proteomes:UP000033633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MELD1 {ECO:0000313|EMBL:KKD01538.1,
RC ECO:0000313|Proteomes:UP000033633};
RA Mathew D.C., Huang C.-C.;
RT "Mercury Reductase activity and rhizosphere competence traits in the genome
RT of root associated Photobacterium halotolerans MELD1.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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:KKD01538.1}.
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DR EMBL; JWYV01000001; KKD01538.1; -; Genomic_DNA.
DR RefSeq; WP_046218862.1; NZ_JWYV01000001.1.
DR AlphaFoldDB; A0A0F5VHL7; -.
DR STRING; 265726.KY46_01585; -.
DR MEROPS; M17.004; -.
DR PATRIC; fig|265726.11.peg.339; -.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000033633; 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:KKD01538.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KKD01538.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000033633}.
FT DOMAIN 272..279
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 425 AA; 45688 MW; 53E9F76FF7089451 CRC64;
MLTVLLSAEP NQGVWGDKAL VSYQQDSVVI HYQDDFVLRR IQQAARQLSA QGATEVSLSG
EGWSYERQWA FYCGFAATRK PVAVQWASMD EDELELLNAR RRSADWVRQV VNATPEDMYP
EKLAQEAISF LKSVAGNHIS HEVLVGDELL AEGWIGTHSV GRASSRPPVM LTLDFNPTGD
PDAPVHACLV GKGITFDSGG YSIKSSAGMV AMKCDMGGAA TVTAALAYAI EQGLKKRVKL
VLCCAENMVA GNAYKLGDIL TYKNGLTVEV VNTDAEGRLV LADGLIKAGE MKAPLIIDAA
TLTGAAMMAV GQDYNAIFSL QPELLRKAQQ LSELVNEPAW PLPLQKWHQN YCPSDYADTA
NSRPVKGGGM GGASNAAAFL SRFVSDDSRW IHFDLASCFR DGADARWAAG ATGLGVANIA
ALLLQ
//
