ID A0A162DJ74_9FLAO Unreviewed; 389 AA.
AC A0A162DJ74;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Peptidase M12A domain-containing protein {ECO:0000259|PROSITE:PS51864};
GN ORFNames=AWE51_22805 {ECO:0000313|EMBL:KZS41238.1};
OS Aquimarina aggregata.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1642818 {ECO:0000313|EMBL:KZS41238.1, ECO:0000313|Proteomes:UP000076715};
RN [1] {ECO:0000313|EMBL:KZS41238.1, ECO:0000313|Proteomes:UP000076715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RZW4-3-2 {ECO:0000313|EMBL:KZS41238.1,
RC ECO:0000313|Proteomes:UP000076715};
RA Wang Y.;
RT "The draft genome sequence of Aquimarina sp. RZW4-3-2.";
RL Submitted (JAN-2016) 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:KZS41238.1}.
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DR EMBL; LQRT01000006; KZS41238.1; -; Genomic_DNA.
DR RefSeq; WP_066312577.1; NZ_LQRT01000006.1.
DR AlphaFoldDB; A0A162DJ74; -.
DR STRING; 1642818.AWE51_22805; -.
DR OrthoDB; 8455098at2; -.
DR Proteomes; UP000076715; 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 Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
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; ZINC METALLOPROTEINASE NAS-29; 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 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:UP000076715};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211}.
FT DOMAIN 98..288
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT ACT_SITE 192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 389 AA; 43151 MW; 2A49E48CB66C0004 CRC64;
MKTKNLINLA KVSALSLGLF FTSCSNESIE DLPEETGGEQ EQLVDKYFKG DLIQVEDIGN
NTFKFGDVLF DSAQLSDEIV AYDANPEPGA GLSSDPKLGL AGGVRKWPNN TIIYVLDNSL
SSNQRQVTFD AMDEWKNKTN IRFKERTNES FYVTIRNSGA QCNCASASLG VQGTRGTINM
GVRTGFGVMT HEIGHTLGYL HEQNRSDRDQ FVRIFPENIQ DGAISQFRVD NNSVNPGRFD
VESIMIYSSF TFSKNGQPVM LELDGSRIPF RSRLSAGDIA GTNQLYPGGD GGDGGGDTDT
CEGVDEWVRG RQYTVGDRVT YRGSLYERDF SRWNRIKECD ATTPQDICEG VAAYNRGTRY
RAGDRVTFQG FLYELQSNGR WSNLGQCAN
//