ID A0A1N7RHR4_9BACT Unreviewed; 563 AA.
AC A0A1N7RHR4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Peptidase family M1 {ECO:0000313|EMBL:SIT34514.1};
GN ORFNames=SAMN05421788_11710 {ECO:0000313|EMBL:SIT34514.1};
OS Filimonas lacunae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Filimonas.
OX NCBI_TaxID=477680 {ECO:0000313|EMBL:SIT34514.1, ECO:0000313|Proteomes:UP000186917};
RN [1] {ECO:0000313|Proteomes:UP000186917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21054 {ECO:0000313|Proteomes:UP000186917};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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; FTOR01000017; SIT34514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7RHR4; -.
DR STRING; 477680.SAMN05421788_11710; -.
DR Proteomes; UP000186917; Unassembled WGS sequence.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09603; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
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; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 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:UP000186917};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|PIRSR:PIRSR634015-3}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..563
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012162014"
FT DOMAIN 287..480
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634015-3"
SQ SEQUENCE 563 AA; 63592 MW; AABE77D727ACEB8C CRC64;
MIMYSIRLFI SACISLLAGV LLTGSALAQK PAYTHADTLR GSITPERSWW NVLYYAITVK
PDEGSKTITG KNSLRYQVTQ ANKGRKMQLD LQKPLVIDSV LWDGIQRVPF EKEGNAWHVW
MPEQQKGSIH RVDIYYGGKV HEAIRPPWDG GWVWGKDSLG RPYMTVACQG LGASIWYPCK
DHQSDEPDSG ASLTMIVPDS LVAVGNGRLQ HKQSNGDGTT TYTWAVVNPI SNYCIIPYIG
KYVNFSEVYN GEKGPLSVNY WVLDYNQARA KEYMPTQVHN MLKSFEYWMG PYPFYEDGYQ
LIDASHTGME HQSAVSYGNR YAFGYRGRDQ SNSGLGLKFD FIIIHESGHE WFGNNITTND
LADMWVHESF TNYSETLFAD YIFGEEAGNA YNYGIRAGIR NDAPIIPVYG VNAQGSGDMY
PKGGNMLHTI RHGMGNDSLF RSIIRGLNST FYHTTVNAAD IENYISKRAG FDYSKVFSQY
LLTTQIPRFE YYFSADKKQV SYRYANCIKG FTMPLLLQQA GVKIKLIPAD SWKSQPVNSE
QAALFTPDAI QKMYYLKVVE GAQ
//
