ID   A0A2S2E643_9ALTE        Unreviewed;       819 AA.
AC   A0A2S2E643;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Membrane alanyl aminopeptidase {ECO:0000313|EMBL:AWL13103.1};
DE            EC=3.4.11.2 {ECO:0000313|EMBL:AWL13103.1};
GN   ORFNames=HMF8227_02651 {ECO:0000313|EMBL:AWL13103.1};
OS   Saliniradius amylolyticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Saliniradius.
OX   NCBI_TaxID=2183582 {ECO:0000313|EMBL:AWL13103.1, ECO:0000313|Proteomes:UP000245728};
RN   [1] {ECO:0000313|EMBL:AWL13103.1, ECO:0000313|Proteomes:UP000245728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF8227 {ECO:0000313|EMBL:AWL13103.1,
RC   ECO:0000313|Proteomes:UP000245728};
RA   Kang H., Kang J., Cha I., Kim H., Joh K.;
RT   "Salinimonas sp. HMF8227 Genome sequencing and assembly.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP029347; AWL13103.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S2E643; -.
DR   KEGG; salh:HMF8227_02651; -.
DR   OrthoDB; 9814383at2; -.
DR   Proteomes; UP000245728; Chromosome.
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:AWL13103.1};
KW   Hydrolase {ECO:0000313|EMBL:AWL13103.1};
KW   Protease {ECO:0000313|EMBL:AWL13103.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245728};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..819
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015728350"
FT   DOMAIN          386..592
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   REGION          798..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..812
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   819 AA;  94949 MW;  A66E2A694304C43B CRC64;
     MFKRAIALSA LLMTGLADPA AASAIRQTKG DFEDKFRQLD ESLPTPNVYR NAAGAPGHQY
     WQQQVDYDID ATLDEDKRRL EAKIQIRYQN NSPDTLRYLW LQLEQNKYLK DSIAEAGSAF
     AGIGRRGPAT QAGDGDTPAR LSLGELRRQQ FMEDNQLGYD IDQLVDGNGE PLHHVIVGTN
     MRVDLNQPLK PGESVRFSMN YAYNIVEEDA VSARAGYEHF PDDEREGGND IFLFAQWFPR
     LHAYTDYEAW TNKPFIGRGE FTLEFGDYDV EMTVPADHIV SSTGTLQNAD DVLTDTQRER
     LEEAANAERP VFVVTEEEAL ENEKEGTDEL KTWHFAADNV RDFAWATSRK FMWDARGYHQ
     GGDEQPLVMA MSFYPKEGGD LWKKYSTESV IHTMEVYSRF SFDYPYPTAQ SVNGPVGGME
     YPMITFNGPR TTLQDDGSRT YSQAEKRFLI GVVIHEIGHI YFPMIVNSDE RQWTWMDEGL
     NSFLDGVAGR EWDPSIPWGV EPRDITGYME SETQVPIMTQ SDSVLRLGPN AYTKPAAALN
     ILRETILGRE LFDFAFREYA QRWKYKRPTP ADFFRTMEEA SGVDLDWFWR GWFYSTDHVD
     ISIERVYKMR LDTEDPDIDF ARQRQHEQDK PLSLTVERNR EEGRQLWIEK NPDISDFYDK
     NDRFTVTNKE RNEYREWLHG LEDWERRVFE RAVEEDKNYY VMEFSNKGGL VMPIILELSF
     EDGSTEMRRI PAEIWRRTPK AVKKLIVTEK DQELVSVTVD PRWETADVDV ENNHYPRRII
     PSRVEAYKAK ERSGKVYRDI MQDSKTELKD PEDEENNDG
//