ID   A0A0C5VCM9_9GAMM        Unreviewed;       414 AA.
AC   A0A0C5VCM9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Peptidase M12A domain-containing protein {ECO:0000259|PROSITE:PS51864};
GN   ORFNames=YC6258_05060 {ECO:0000313|EMBL:AJQ97090.1};
OS   Gynuella sunshinyii YC6258.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Saccharospirillaceae; Gynuella.
OX   NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ97090.1, ECO:0000313|Proteomes:UP000032266};
RN   [1] {ECO:0000313|EMBL:AJQ97090.1, ECO:0000313|Proteomes:UP000032266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC6258 {ECO:0000313|EMBL:AJQ97090.1,
RC   ECO:0000313|Proteomes:UP000032266};
RA   Khan H., Chung E.J., Chung Y.R.;
RT   "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT   YC6258T gen. nov., sp. nov.";
RL   Submitted (JAN-2014) 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}.
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DR   EMBL; CP007142; AJQ97090.1; -; Genomic_DNA.
DR   RefSeq; WP_052830503.1; NZ_CP007142.1.
DR   AlphaFoldDB; A0A0C5VCM9; -.
DR   STRING; 1445510.YC6258_05060; -.
DR   KEGG; gsn:YC6258_05060; -.
DR   PATRIC; fig|1445510.3.peg.5019; -.
DR   HOGENOM; CLU_663527_0_0_6; -.
DR   Proteomes; UP000032266; Chromosome.
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; 2.60.120.380; -; 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   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW   ProRule:PRU01211}; Protease {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032266};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211}.
FT   DOMAIN          101..295
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   REGION          293..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   414 AA;  44940 MW;  05110F46F1597C0A CRC64;
     MKKIIPLTAA ILFVTACNDS GSETASGNGQ DSIWGYSSTG RNLVEIQTSN GQTIKAVDID
     GIAHVGDMML GRTEDLLQHG LTVAENQDQP TAQEKSISRA ATIYPSSGFK WPDGIVPFAL
     NSNLSSAARA DALSAISYWN TNTNVKFIER TNEADYLLIT NGNGCSSYVG KIGGAQAVTL
     AYNCGMAAAI HELGHAVGFE HEQTRSDRDN YVSIYWDNIQ SGMEYNFEKI NTSNRHDVGN
     YDYYSIMHYH AWAFSKNDQP TILPKQDDVD LYTMGMVSEM SAGDLAAVAA IYGDPGNGND
     NSGDNDNDNS GDPDQNQGEQ YSGQLSGSRA TNIQPNGNWF QYQGGTLSAT LSGPDNADFD
     LYLQQWNGRS WVNVAISESY SSSEAISYEA AAGYYQFVVL SYNGSGSYTF TLKR
//