ID A0A0Q6XIP8_9BURK Unreviewed; 650 AA.
AC A0A0Q6XIP8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KQW03042.1};
GN ORFNames=ASC87_01525 {ECO:0000313|EMBL:KQW03042.1};
OS Rhizobacter sp. Root1221.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQW03042.1, ECO:0000313|Proteomes:UP000051465};
RN [1] {ECO:0000313|EMBL:KQW03042.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQW03042.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW03042.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQW03042.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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|ARBA:ARBA00006040, 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:KQW03042.1}.
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DR EMBL; LMDI01000001; KQW03042.1; -; Genomic_DNA.
DR RefSeq; WP_056655492.1; NZ_LMDI01000001.1.
DR AlphaFoldDB; A0A0Q6XIP8; -.
DR STRING; 1736433.ASC87_01525; -.
DR OrthoDB; 9773538at2; -.
DR Proteomes; UP000051465; 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; cd06455; M3A_TOP; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR024077; Neurolysin/TOP_dom2.
DR InterPro; IPR045090; Pept_M3A_M3B.
DR InterPro; IPR001567; Pept_M3A_M3B_dom.
DR PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR Pfam; PF01432; Peptidase_M3; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 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:UP000051465};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..650
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006297720"
FT DOMAIN 222..647
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 650 AA; 71999 MW; 70018746FB806A45 CRC64;
MPWWRSVPIA VAGAWLAASA VAAPYTFPVL DSAARIDRAC SVAMTRARAA ERHLAVRPAD
ATLLGALDGL AQQLEDTMGP VGLLAAVHPD AAVRGAASAC ERRQQAFVSA FLQNARIYRL
LRRLEPVDDI DRRFRQDQLD AFEDAGVALS PSRRLRARQI ARQLARRIQD FERRILEDKR
VVAFTEAELE GVPRAVWAST PKDGQGRYRL GLDAPTYQPV VEYATQRATR ERMWRAGLTQ
GGEANLRTLD DIARLRREEA ALQGFPSYAD FTLRRRMAHD ETTVTAFLAS VQAAVGEREL
ADLSQLQAAQ PGVPLQRWDV PYQVERLRRA RHGVDQEQFR PHFPPDASLD FVFRLAGRLF
GVTFEPQPQP QPLWHPDAHA FSVHDGPGGA YLGTLFVDLY PRPGKYNHAA VWGLRNVSTR
TGRTPAAALV VNFNRNGLNL DELETLLHEF GHALHGLLSA TRYASQGGTN VQLDFVEAPS
QMLEDWVYDP KVMALFQAVC ATCPPVPDGL LARAFAAREF GKGVQFARQR LFASYDLALY
GRRPAVPLAL WREMESATPL GHVPGSMFPA GFAHIAGGYG AGYYGYLWSL VLAEDLRTAF
AGDRLSAETG RRYRDTVLSQ GGQADAGELL RRFLGRPPTN EAFFKALSRP
//