ID Q2YNB5_BRUA2 Unreviewed; 512 AA.
AC Q2YNB5;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Bacterial sugar transferase {ECO:0000313|EMBL:CAJ10758.1};
GN OrderedLocusNames=BAB1_0802 {ECO:0000313|EMBL:CAJ10758.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ10758.1, ECO:0000313|Proteomes:UP000002719};
RN [1] {ECO:0000313|EMBL:CAJ10758.1, ECO:0000313|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000313|EMBL:CAJ10758.1,
RC ECO:0000313|Proteomes:UP000002719};
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG Microbial Genomics Group;
RG Lawrence Livermore National Laboratory;
RG and the Genome Analysis Group;
RG Oak Ridge National Laboratory;
RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
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}.
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DR EMBL; AM040264; CAJ10758.1; -; Genomic_DNA.
DR RefSeq; WP_002963917.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YNB5; -.
DR STRING; 359391.BAB1_0802; -.
DR GeneID; 58776097; -.
DR KEGG; bmf:BAB1_0802; -.
DR PATRIC; fig|359391.11.peg.3113; -.
DR HOGENOM; CLU_024920_0_1_5; -.
DR PhylomeDB; Q2YNB5; -.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
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; IPR036291; NAD(P)-bd_dom_sf.
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.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Exopolysaccharide synthesis {ECO:0000256|ARBA:ARBA00023169};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002719};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAJ10758.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 318..506
FT /note="Bacterial sugar transferase"
FT /evidence="ECO:0000259|Pfam:PF02397"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 57668 MW; 4B3C500E6DBE1FD8 CRC64;
MQDTQARSPS GGEAAIAAAS QDSGPQEKTG LSDMARQMAA QYQRETLSPA MLSGMMRLVE
LTLIFATGIL SFAYYVGLNT NLNFYYPLII IAGSALFVML MELNGGYQPG VLRSATRNLR
RVFVNWATVL GALAIAGFLF KISSQFSRGW FIIWAVSAFG VLVISRLFIA WKIRRWARNG
TMERRAIIVG GGTNAESLIR SLEQQPDNDI RICGIFDDRD DRRSPPIVAG YPKIGNIDDL
IEFARIAHID LLIISLPISA ELRVLSLLKK LWVLPVDIRL SALNNHLRFH PRAYSYVGSV
PMLDIFDKPI NDWDSVAKRI FDIVFSLLGI ILLSPIMLAT AIAIKLDSKG PVIFKQKRHG
FNNEVINVWK FRSMYADKCD PAAKQVTTKN DPRVTRVGRF IRKTSIDELP QFFNALSGTL
SLVGPRPHAV AAHSHNVLFN EVVDGYFARH RVKPGVTGWA QINGWRGEID NAEKIRMRTE
YDLFYIENWS LWFDLKILFL TPIRLLNTEN AY
//
