ID Q2KTI3_BORA1 Unreviewed; 399 AA.
AC Q2KTI3;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Probable amidohydrolase/peptidase {ECO:0000313|EMBL:CAJ51028.1};
GN OrderedLocusNames=BAV3418 {ECO:0000313|EMBL:CAJ51028.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ51028.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ51028.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ51028.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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DR EMBL; AM167904; CAJ51028.1; -; Genomic_DNA.
DR RefSeq; WP_012419054.1; NC_010645.1.
DR AlphaFoldDB; Q2KTI3; -.
DR GeneID; 41395250; -.
DR KEGG; bav:BAV3418; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_4; -.
DR OrthoDB; 8875216at2; -.
DR Proteomes; UP000001977; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd05666; M20_Acy1-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF005962; Pept_M20D_amidohydro; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001977}.
FT DOMAIN 186..279
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 399 AA; 43507 MW; 5603893C1BFC7AC3 CRC64;
MKTIDEIQRA HGELTALRRD IHAHPELAFQ ETRTSNLVAE RLRALGLEVH TGLGRTGVVG
VLRAGSGKKS IGLRADMDAL PMPEENRFAH RSTIAGRMHG CGHDGHTAIL LGAAQYLAAH
PDFDGTVNFI FQPAEEGGNA GARAMMQDGL FERFPCDAIF GLHNMPGMPV NQFGFRAGPM
MASSNRWDIV IKGLGGHAAQ PHGAVDPIVI AAEMVQSLQT VISRGRDPLD PAVLSITQIH
AGDAYNVIPG EAVLRGTVRT YTLDALDKIE ADMRRIATTL PQVYGGTGEL HFVRAYPPLL
NWEQETAFAL RVAEETFGKE HVNPSVMQSM AAEDFSFFLE KVPGCYLFLG NGDGDHRQQP
YHGMGPCQLH NPNYDFNDAL LPVGASYWVK LVQAFLPKN
//
