ID F4QTP0_9CAUL Unreviewed; 258 AA.
AC F4QTP0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Astacin Peptidase family M12A family protein {ECO:0000313|EMBL:EGF89190.1};
GN ORFNames=ABI_45370 {ECO:0000313|EMBL:EGF89190.1};
OS Asticcacaulis biprosthecium C19.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF89190.1, ECO:0000313|Proteomes:UP000006512};
RN [1] {ECO:0000313|Proteomes:UP000006512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Draft genome sequence of Brevundimonas diminuta.";
RL Submitted (MAR-2011) 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; GL883081; EGF89190.1; -; Genomic_DNA.
DR RefSeq; WP_006275311.1; NZ_GL883081.1.
DR AlphaFoldDB; F4QTP0; -.
DR STRING; 715226.ABI_45370; -.
DR eggNOG; COG3170; Bacteria.
DR HOGENOM; CLU_1076239_0_0_5; -.
DR OrthoDB; 9783144at2; -.
DR Proteomes; UP000006512; 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; 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.
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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..258
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003316874"
FT DOMAIN 19..146
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT ACT_SITE 125
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 258 AA; 29172 MW; A0C008546CAC5BDC CRC64;
MRAWFFLVLL LPLPAQAGAV MKSTKPWSNA TVPYQLSADI LKTAYTQSKD CTGWAKWKAS
PAHKACKAMN DWHRRTGVRF VARDGLGSVQ IYLNPHATSA TVGQLPIGNQ VNIQPGANYG
SILHEFGHTL GLAHEHQRAD RATYLNLQPF LQTYLETCGM KLDTVCNDVR SAFPEREMRL
TSDYDPCSLM HYLANQGPRH KEDPRWSRIF TLTTKGKAAE KACLPQFAKL EKRCRKIVQK
CAISDRDAWT VRRFHGLE
//
