ID A0A1X9Z1T5_9SPHI Unreviewed; 397 AA.
AC A0A1X9Z1T5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Peptidase M12A domain-containing protein {ECO:0000259|PROSITE:PS51864};
GN ORFNames=CA265_05170 {ECO:0000313|EMBL:ARS39098.1};
OS Sphingobacteriaceae bacterium GW460-11-11-14-LB5.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae.
OX NCBI_TaxID=1986952 {ECO:0000313|EMBL:ARS39098.1, ECO:0000313|Proteomes:UP000194429};
RN [1] {ECO:0000313|Proteomes:UP000194429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ray J., Price M., Deutschbauer A.;
RL Submitted (MAY-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}.
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DR EMBL; CP021237; ARS39098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9Z1T5; -.
DR KEGG; sbx:CA265_05170; -.
DR OrthoDB; 8455098at2; -.
DR Proteomes; UP000194429; 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 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; 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|PROSITE-ProRule:PRU01211};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211};
KW Reference proteome {ECO:0000313|Proteomes:UP000194429};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211}.
FT DOMAIN 88..283
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT ACT_SITE 178
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 397 AA; 44039 MW; A2EB6BED5089F034 CRC64;
MKKIYYIFAL LIIFTSACKK EGSIKGEQPQ APGKTITYHL KNGGQVTVAI NNKGEYVVGG
DVILSKDQIA YLEYNKIGNG KETTPRSTFT AEYQKLWPGG IIYYVINDAT HSSDILSAIN
AWESSTPIRF VQRTNQANYI NFAGLPENGA GDSKLGMIGG EQAIRLAASA DESTVIHEIG
HAVGLMHEQT RADRDQYINI DFSNINADWT DQYKTYDVLG RSGFQIGTFD FNSIMLYRSN
VAEARVGSNT SPQMTRKDGT TWGDSDHLSQ GDIDGVNYLY RPIYVKLVSV YNEDGSYYNS
SITNEDARFE YFISLEFFSD ANFNTPIDLV NPVRIRYINS FGSLQGSGAD IGELTAPVGS
HSVYLGTALT EYSSEYGNYR YYSSSSFALT SGIGYRY
//
