ID A0A091B458_9GAMM Unreviewed; 724 AA.
AC A0A091B458;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Peptidase M3A/M3B catalytic domain-containing protein {ECO:0000259|Pfam:PF01432};
GN ORFNames=P873_01670 {ECO:0000313|EMBL:KFN47378.1};
OS Arenimonas composti TR7-09 = DSM 18010.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1121013 {ECO:0000313|EMBL:KFN47378.1, ECO:0000313|Proteomes:UP000029391};
RN [1] {ECO:0000313|EMBL:KFN47378.1, ECO:0000313|Proteomes:UP000029391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TR7-09 {ECO:0000313|EMBL:KFN47378.1,
RC ECO:0000313|Proteomes:UP000029391};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas composti.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003435};
CC Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC -!- SIMILARITY: Belongs to the peptidase M3 family.
CC {ECO:0000256|RuleBase:RU003435}.
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:KFN47378.1}.
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DR EMBL; AWXU01000066; KFN47378.1; -; Genomic_DNA.
DR RefSeq; WP_026816007.1; NZ_AWXU01000066.1.
DR AlphaFoldDB; A0A091B458; -.
DR eggNOG; COG0339; Bacteria.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000029391; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06456; M3A_DCP; 1.
DR Gene3D; 1.10.1370.40; -; 3.
DR InterPro; IPR034005; M3A_DCP.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003435};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003435};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW Reference proteome {ECO:0000313|Proteomes:UP000029391};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT DOMAIN 272..718
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 724 AA; 78856 MW; A6E863A046FC69CE CRC64;
MNKSLVAAPL ALAIALAVGG CQQPAGEASA APTTAADAAT DAVTENPFFA PSTLQYQFPR
FDLIRDEHYQ PALERGMAEQ IAEVRAIADN PEAPSFDNTI VAMENSGALL NRVGAVFFNL
AGAHTNDAIK AVQAEMAPKM AAHQDAILLD AALFARIKTL YDGRAELGLD AESQRLLERY
YTDFVRAGAN LSDADKDVLR GYNAELATLS TKFSQNVLNE VNASGVWVDD VARLDGLSDE
AITAAAEAAK AAGQEGRYLI ALMNTSGQPP LASLTDRALR QEIMAASLAR GTRGNEFDNR
EIIARVARLR AERAALLGYD SHAAYIIEDE TAGTVAAVNK LLSDLAPAAV ANARREAADM
QAIIDAEGGG FQLEAADWAF YAEKVRQQRY DFDESQLRPY FEMNRVLEDG VFYAAGQLYG
LSFKERTDLP VYQQDVRVWE VFEADGSSLG LFIGDFYARA SKRGGAWMNA YVPQNGLTGT
HPVVGNHLNI PKPAAGQPTL LTFDEVTTMF HEFGHALHGL FSSTRYPQFA GTSVPRDFVE
YPSQVNEMWA TWPSVLANYA KHYQTGEPIP QALLDKVLAA EQYGQGHATT EYLAASLLDQ
AWHQLKPDQV PTDALAFEAQ ALKAAGVDYA PVPPRYRSTY FSHIMGGYSA GYYAYLWSEV
LDAESVEWFK ENGGLSRANG DHFRATLLSK GGSVDAMQLF RDFRGRDPQV GPLLRRRGLE
TGGN
//
