ID A0A1H3W1C6_9FLAO Unreviewed; 608 AA.
AC A0A1H3W1C6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Peptidase family M1 {ECO:0000313|EMBL:SDZ80214.1};
GN ORFNames=SAMN05421540_101356 {ECO:0000313|EMBL:SDZ80214.1};
OS Psychroflexus halocasei.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Psychroflexus.
OX NCBI_TaxID=908615 {ECO:0000313|EMBL:SDZ80214.1, ECO:0000313|Proteomes:UP000198820};
RN [1] {ECO:0000313|EMBL:SDZ80214.1, ECO:0000313|Proteomes:UP000198820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23581 {ECO:0000313|EMBL:SDZ80214.1,
RC ECO:0000313|Proteomes:UP000198820};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634015-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634015-3};
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DR EMBL; FNQF01000001; SDZ80214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3W1C6; -.
DR STRING; 908615.SAMN05421540_101356; -.
DR Proteomes; UP000198820; Unassembled WGS sequence.
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 Metal-binding {ECO:0000256|PIRSR:PIRSR634015-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000198820};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..608
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011633386"
FT DOMAIN 342..494
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT ACT_SITE 435
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-1"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 608 AA; 70515 MW; 71694EBA409429C7 CRC64;
MLRYFFSLNL FIFSLVAFAQ NNTSYWQQHV EYTMNIDFDV KKYQYDGEQE LVYTNNSPDT
LYKAYYHLYF NAFQPGSEMD VRSRSIKDPD RRVTDRISKL SEDEIGFIKV KSLMQDGENA
SYQVKGTVLE VRLANPILPG NSTTFDMKFE GQVPVQIRRS GRNSAEGVAL SMTQWYPKLA
EYDFEGWHAD PYIGREFHGV WGNFDVKIKI DKDYILGGTG YLQNPNEIGY GYEEEGVKVK
RKGRKLTWHF VAPGVHDFTW AADPEYIHDK RTAYDGTTLH FLYKDNPDIK ENWVNLQDKT
EGLLKYFNKH IGQYPYKQYS VIQGGDGGME YAMSTLITGE RSFGSLVGVT AHELAHAWFQ
HLLATNELRH EWMDEGFTSY MSTLAENAVF EKDPDFPHKN SYNSYIGLAN SGFEHPQTTH
ADRYKYNAAY GASAYSKGAV FLSQLGYLIG EDNLQKTIHR YYDEWKFKHP TPNDFIRIAE
KVSDAELSWY LNDWTRTTNQ IDYAITSVQN DVTQNTIIVN LERKGLMPMP LEVEVTYEDG
STQMIYIPLR MMRWTKPNQD VVEDDWPWAF PTYKLELPVT NFAITKIEID PSQLMADIDR
TNNVKVLK
//
