ID B0SQM0_LEPBP Unreviewed; 396 AA.
AC B0SQM0;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=NodB homology domain-containing protein {ECO:0000259|PROSITE:PS51677};
GN OrderedLocusNames=LEPBI_I1571 {ECO:0000313|EMBL:ABZ97678.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ97678.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ97678.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
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DR EMBL; CP000786; ABZ97678.1; -; Genomic_DNA.
DR RefSeq; WP_012388557.1; NC_010602.1.
DR AlphaFoldDB; B0SQM0; -.
DR STRING; 456481.LEPBI_I1571; -.
DR KEGG; lbi:LEPBI_I1571; -.
DR HOGENOM; CLU_692227_0_0_12; -.
DR OrthoDB; 341122at2; -.
DR BioCyc; LBIF456481:LEPBI_RS07745-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10917; CE4_NodB_like_6s_7s; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001847};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..385
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 396 AA; 45851 MW; 114B0CF9714B6D50 CRC64;
MSLDPTNEEK EIQDIVHELS KDIEKDRLFA KKLRRFAFIS ALAFVGATVL VLTGYLLYLS
LSVTKLETEV KEKERSLREL EQSLFSLMYQ EQLREENALA GETEPDTELA KQVEENIEFL
KEVSANTKGR NILRGNEAHK EIALTFDLAT GEELPVLYNY IKEHKIKVTL FLSNERPSDT
NGSFFVRQNL DYIKRMAKTG SVEFGNHTWS HFNYQRSVTE TSLKKRMVLD YLSKSVLDLP
RMAEELKRVE DTFQSLTKQE LKKYYRLPYG ALSQLILDAH ASLGYTDHIM WSNNPKGSLD
LPDYISKQFL YKKTSKGKKE VVKNPHYKTG EETLTFLDNW EKADPHGMNG AIILMHLGGP
RKFDKLIYIL PTFIERMKEK GYHFVTLSEV LNNQKD
//
