ID A0A2N1FDW0_9FLAO Unreviewed; 344 AA.
AC A0A2N1FDW0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Peptidase M12 {ECO:0000313|EMBL:PKH53095.1};
GN ORFNames=CXF68_19710 {ECO:0000313|EMBL:PKH53095.1};
OS Tenacibaculum sp. Bg11-29.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=2058306 {ECO:0000313|EMBL:PKH53095.1, ECO:0000313|Proteomes:UP000233844};
RN [1] {ECO:0000313|EMBL:PKH53095.1, ECO:0000313|Proteomes:UP000233844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bg11-29 {ECO:0000313|EMBL:PKH53095.1,
RC ECO:0000313|Proteomes:UP000233844};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01211}.
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:PKH53095.1}.
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DR EMBL; PJBB01000003; PKH53095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1FDW0; -.
DR OrthoDB; 8455098at2; -.
DR Proteomes; UP000233844; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04280; ZnMc_astacin_like; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR034035; Astacin-like_dom.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF850; METALLOENDOPEPTIDASE; 1.
DR Pfam; PF01400; Astacin; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU01211};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211};
KW Reference proteome {ECO:0000313|Proteomes:UP000233844};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..344
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014923071"
FT DOMAIN 97..291
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 161..183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 344 AA; 38626 MW; 70C3AC97ED085364 CRC64;
MKTKCYYALL ISLSLFTACN ENENSENLTN QTAPSLKTEL AFPGQSGEIK KGFYQGVPVT
YEVIEGQYVM GGDVILPKEH VYDSLDGLVL EPGQKPNAKK RSAGATTNRW PNSTVYYTIG
SAPNKSYVRN AIAHWQSKTN LKFVKRTNQP NYISFDGGSG CSSAIGMQGG RQVVTLGTNR
QPCQQGSVIH EIGHAIGLFH EQSRSDRDSY VKIIDENIIP NMKYNFDKYS IRYHGSDNTP
FDFNSIMMYA DWSFSKNGRP TITRLNGSSY STQRNGLSPR DIAGIKKMYP SSAGGDTSGG
TTYHNNQDYT LHGLKVHRQN NLWWFHDGKD WRQVELKGTS WYYV
//
