ID A0A0F4PNS8_9GAMM Unreviewed; 431 AA.
AC A0A0F4PNS8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Aminopeptidase B {ECO:0000313|EMBL:KJY98559.1};
DE EC=3.4.11.23 {ECO:0000313|EMBL:KJY98559.1};
GN ORFNames=TW72_12575 {ECO:0000313|EMBL:KJY98559.1};
OS Pseudoalteromonas ruthenica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=151081 {ECO:0000313|EMBL:KJY98559.1, ECO:0000313|Proteomes:UP000033664};
RN [1] {ECO:0000313|EMBL:KJY98559.1, ECO:0000313|Proteomes:UP000033664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3137 {ECO:0000313|EMBL:KJY98559.1,
RC ECO:0000313|Proteomes:UP000033664};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJY98559.1}.
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DR EMBL; JXXZ01000010; KJY98559.1; -; Genomic_DNA.
DR RefSeq; WP_045979682.1; NZ_PPSV01000023.1.
DR AlphaFoldDB; A0A0F4PNS8; -.
DR GeneID; 58229327; -.
DR PATRIC; fig|151081.8.peg.2347; -.
DR eggNOG; COG0260; Bacteria.
DR OrthoDB; 9809354at2; -.
DR Proteomes; UP000033664; 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:KJY98559.1}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KJY98559.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000033664}.
FT DOMAIN 275..282
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 431 AA; 46042 MW; 8AF6B7C16D812BB4 CRC64;
MSQQFLVHLS EQAAPSHWGE SASVSFNEQG ATVHLSEDET LKNVQKAGRA IANQGVKAVQ
LSGDTWCTES QWAFYQGFVS PKVLDGVSFV DNDQSDIKEL QALKQAATWM RQMINGTAEE
IYPESLAEKA GEFIQSLAPE HVSYQIIKGE ALKEQQWIGI YEVGRGSERP PVLLELDFNP
TGDDAAEVAS ALVGKGITFD SGGYSIKPSE GMLGMKCDMG GAATVTAGLA LAISRGLDKR
VKLYLCCAEN LISGHAYKLG DILTYKNGTT VEIVNTDAEG RLVLADGLMA ASESGAKTII
NAATLTGAAL VAVGQEYNAL FGLDKDMVRD VEGFAKEEFE GAWPLPLEKF HQHNCPSPYA
DTANSRPQKG GGFGGASNAA GFLSRFVRDE GQGWVHIDLA AAFQTSATGM WAAGATTQGM
RTVARTLQEK S
//
