ID B0SRP3_LEPBP Unreviewed; 466 AA.
AC B0SRP3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Putative undecaprenyl-phosphate galactose phosphotransferase putative membrane protein {ECO:0000313|EMBL:ABZ97838.1};
DE EC=2.7.8.6 {ECO:0000313|EMBL:ABZ97838.1};
GN OrderedLocusNames=LEPBI_I1732 {ECO:0000313|EMBL:ABZ97838.1};
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:ABZ97838.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ97838.1, 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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC {ECO:0000256|ARBA:ARBA00006464}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000786; ABZ97838.1; -; Genomic_DNA.
DR RefSeq; WP_012388716.1; NC_010602.1.
DR AlphaFoldDB; B0SRP3; -.
DR STRING; 456481.LEPBI_I1732; -.
DR KEGG; lbi:LEPBI_I1732; -.
DR HOGENOM; CLU_024920_0_1_12; -.
DR OrthoDB; 9808602at2; -.
DR BioCyc; LBIF456481:LEPBI_RS08555-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047360; F:undecaprenyl-phosphate galactose phosphotransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR003362; Bact_transf.
DR InterPro; IPR017475; EPS_sugar_tfrase.
DR InterPro; IPR017473; Undecaprenyl-P_gluc_Ptfrase.
DR NCBIfam; TIGR03025; EPS_sugtrans; 1.
DR NCBIfam; TIGR03023; WcaJ_sugtrans; 1.
DR PANTHER; PTHR30576; COLANIC BIOSYNTHESIS UDP-GLUCOSE LIPID CARRIER TRANSFERASE; 1.
DR PANTHER; PTHR30576:SF0; UNDECAPRENYL-PHOSPHATE N-ACETYLGALACTOSAMINYL 1-PHOSPHATE TRANSFERASE-RELATED; 1.
DR Pfam; PF02397; Bac_transf; 1.
DR Pfam; PF13727; CoA_binding_3; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001847};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABZ97838.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 279..458
FT /note="Bacterial sugar transferase"
FT /evidence="ECO:0000259|Pfam:PF02397"
SQ SEQUENCE 466 AA; 53205 MW; 7F8182AED9D6A6A0 CRC64;
MLKERSQSFK LLFLVTDFFI GLTSFLTAYI FRYYLSPDSS FQIQTIDPLN YLILGIVLGF
SQVFSFLSID LYHPRRGLSF SDELFAIISG VILNLLVVLS LLFFFRGESF SRLVIGYFAI
CTIILTSFSH FLLRALMQYL RSKGYNLKSV LIIGTGKSAI NFSKTLQKHS IYGYTVKGFV
SGKKNLSPKS VQTVTTTSKL ENYVENNLID LIVYALSHEE GDSLKEVIDI ADFHGIDLKV
IPSYEEIVTA KGRVEVLDGI PIISIRNIPL RLGYNLVLKR SFDILFSLFF ILLFSPFYIL
IALLVKLTSK GPVFYKQERV GLDNKVFGMI KFRSMVVQAK EKSDTLWTVK DDPRVTSIGA
ILRKLSLDET PQFFNVLLGD MSVVGPRPER PFYVEKFRNE HHQYMRRHAA KAGITGWAQV
QGFRGDTSIE KRIEADIFYI ENWSLLLDIK IILLTPLKAI IDRNAY
//
