ID S4XXV3_SORCE Unreviewed; 661 AA.
AC S4XXV3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Peptidase M12A domain-containing protein {ECO:0000259|PROSITE:PS51864};
GN ORFNames=SCE1572_28165 {ECO:0000313|EMBL:AGP38007.1};
OS Sorangium cellulosum So0157-2.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP38007.1, ECO:0000313|Proteomes:UP000014803};
RN [1] {ECO:0000313|EMBL:AGP38007.1, ECO:0000313|Proteomes:UP000014803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP38007.1,
RC ECO:0000313|Proteomes:UP000014803};
RX PubMed=23812535; DOI=10.1038/srep02101;
RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT milieu.";
RL Sci. Rep. 3:2101-2101(2013).
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; CP003969; AGP38007.1; -; Genomic_DNA.
DR AlphaFoldDB; S4XXV3; -.
DR STRING; 1254432.SCE1572_28165; -.
DR KEGG; scu:SCE1572_28165; -.
DR PATRIC; fig|1254432.3.peg.6371; -.
DR eggNOG; COG3170; Bacteria.
DR HOGENOM; CLU_414984_0_0_7; -.
DR Proteomes; UP000014803; 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); 2.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR PANTHER; PTHR10127:SF887; ASTACIN-LIKE METALLOENDOPEPTIDASE; 1.
DR PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR Pfam; PF01400; Astacin; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
DR PROSITE; PS51864; ASTACIN; 2.
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 Zinc {ECO:0000256|PROSITE-ProRule:PRU01211}.
FT DOMAIN 87..166
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 366..467
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT ACT_SITE 369
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 368
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 661 AA; 69949 MW; BAA5D139DCFFCF94 CRC64;
MLSGCVAEGS DDDLPGGAGA VASCGLTDEY EVLDTGHITK GDIIVGKIDE LTAACVEGRH
YPLDGKPRAA SGGSGLEGYP AAGPLGVGTV SASLKWPAAV VPYQIDPGLP SPSRVLDAID
HWQSLTPISF VPRTNQSDYV YFTNGNACAS SVGRQGGRQD IVLSTGKSPG AIVASSISNS
DSVYTWYNDG MVSAGTSSGL DDKLPQYPYT LPPGYQISQI RGIAIAKSNN HVYVWYSDGK
VSSGTTADLD KYFPPTPFSL PPGKTALDIV EMDISMNDHV YTWFDDGTAT IGNSTDLDAY
HAPYAYALPP GYTTSMIAGL GIAGSSDWIY AWYTDGKASS GTSADFDGHS APYAYDTPGN
CGLSAAIHEI GHAVGLQHEQ SRCDRDSFVR IFSDNIKPGK EGNFDKICGA SWDDIGGYNT
TSIMQYRSHS FSKNGSPTIL AKTPAGQPVS SASVVDMAIA SNDWIYTWWN DGTATAGASN
DLERHLSRYE YELPPGYSIS DIAGIGIAKS NNHVYVWYKD GKVSSGTSAD FDAYLAPYSY
TLPSGYTPAD IIAVDIASND HVYVWYANGK ASSGTSADLD KYIAPYSFTV ATGRTIGQIL
GIGFAANDWL YAWYTTGQAS AGNSANFDAH LALYPFAGRL GMLNPSSGLN TGDVAAIDIM
Y
//
