ID B2FNV1_STRMK Unreviewed; 406 AA.
AC B2FNV1;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:CAQ45607.1};
GN OrderedLocusNames=Smlt2104 {ECO:0000313|EMBL:CAQ45607.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ45607.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ45607.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ45607.1,
RC ECO:0000313|Proteomes:UP000008840};
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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DR EMBL; AM743169; CAQ45607.1; -; Genomic_DNA.
DR RefSeq; WP_012479985.1; NC_010943.1.
DR AlphaFoldDB; B2FNV1; -.
DR EnsemblBacteria; CAQ45607; CAQ45607; Smlt2104.
DR KEGG; sml:Smlt2104; -.
DR PATRIC; fig|522373.3.peg.2000; -.
DR eggNOG; COG1473; Bacteria.
DR HOGENOM; CLU_023257_0_1_6; -.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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:UP000008840}.
FT DOMAIN 203..298
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 406 AA; 43214 MW; 2723D3DFE9581936 CRC64;
MSGENSVSPG HARRDPASIG VLPEIAARAE AAIAIRHDLH RHPELAFEEH RTSARVAELL
QQWGYEVTTG LGGTGVVGTL QRGQGGRRLG LRADIDALPI HEDSGLAYAS QNEGLMHACG
HDGHTAILLS AAHYLAHHGN IDGTLQLVFQ PAEETGSGAS KMIADGLFER FSVDAIYGLH
NWPGVPVGHF GFVDGPAMAS VDWARLKVIG KGGHGAEPQG SVDPILVAAH IITALQSVVS
RNVDPRQMGV VTVGSIHGGQ AANVIPDVVE LKLTVRAYLP EVRDTLRRRV TGIAEQTAAA
FGARAEIEFP RGFPSVINHP QQTAYIREVA LQGFGSEHVV PEFAPRTASE DFAFLLQARP
GSFVFVGNGD SAPLHSPRYV FNDAAIAPAA SLWARLAEDY LVKDVA
//
