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Database: UniProt
Entry: U1L1Z2_9GAMM
LinkDB: U1L1Z2_9GAMM
Original site: U1L1Z2_9GAMM 
ID   U1L1Z2_9GAMM            Unreviewed;       815 AA.
AC   U1L1Z2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Aminopeptidase {ECO:0000313|EMBL:ERG26951.1};
GN   ORFNames=PMAN_06482 {ECO:0000313|EMBL:ERG26951.1};
OS   Pseudoalteromonas marina DSM 17587.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1117316 {ECO:0000313|EMBL:ERG26951.1, ECO:0000313|Proteomes:UP000016528};
RN   [1] {ECO:0000313|EMBL:ERG26951.1, ECO:0000313|Proteomes:UP000016528}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17587 {ECO:0000313|Proteomes:UP000016528};
RX   PubMed=22535931; DOI=10.1128/JB.00265-12;
RA   Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA   He H.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of type strains of seven species of the marine bacterium
RT   Pseudoalteromonas.";
RL   J. Bacteriol. 194:2746-2747(2012).
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:ERG26951.1}.
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DR   EMBL; AHCB02000012; ERG26951.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1L1Z2; -.
DR   Proteomes; UP000016528; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd09604; M1_APN_like; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   4: Predicted;
KW   Aminopeptidase {ECO:0000313|EMBL:ERG26951.1};
KW   Hydrolase {ECO:0000313|EMBL:ERG26951.1};
KW   Protease {ECO:0000313|EMBL:ERG26951.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..815
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004615294"
FT   DOMAIN          376..583
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   REGION          796..815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   815 AA;  94188 MW;  8C394F1E0A35F4AB CRC64;
     MKKISLTLSA LLLPMVMSGS AIASSVEQTK GSFVDKFRQL DEALPTPNVY RSAAGEPGEN
     YWQQKVNYDI DVKLDEKKRR LSASQSIEYK NNSPHTLKYL WLQLDQNIFK SDSIAETTKT
     FKSTLQSLPA QKPAKLSLGQ LRRQQFMSDN ELGFAISNVK DEDGKALRVT IVDTLMRIDL
     NEPLKPGKEV EFSMDFAFNI VEEDAVGARS GYEHFEKDGN DIFLLAQWFP RLAAYTDYEA
     WTNKAFLGSG EFTLEFGDYD VEITVPADHI VSATGKLDNP SKVLTSTQRK RLKQSETAKR
     PVFIVTEEEA LENEKEGTDK TKTWRFKADN VRDFAWASSR KFMWDAKGYQ QGGDVQPLVM
     AMSFFPKEGG DLWKKYSTES VVHTMEVYSK YSFDYPYPTA QSVNGPVGGM EYPMITFNGP
     RTKLQDDGTR TYSQSEKRFL IGVVIHEVGH IYFPMIVNSD ERQWTWMDEG LNSFLDGVAG
     REWDPTIPWG VEPRDIVSYM KSEVQVPIMT QSDSVLRLGP NAYTKPAAAL NILREVILGR
     DLFDFAFKEY AQRWKYKRPT PADFFRTMEE ASGVDLDWFW RGWFYTTDHV DISLDKVYQL
     RLDTKNPDID YSRLRDIEAD KPTSLFVERN RAEGKKTWVE KNPDITDFYD ENDRFTVTNK
     ERNAYNKFLK GLEPWERKTL DRALSDDQNY YVMEFSNLGG LVMPILLELT YEDGTKEERY
     IPAEIWRRNH KNVQKLIVTD KNKPLVSVSV DPRWETADVD VENNNYPRRI IPSRIEVFKK
     SKSKAKVSRD IMQDIKTELK SDEKKDEKDE VEEQQ
//
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