ID A0A160FSP4_9BURK Unreviewed; 486 AA.
AC A0A160FSP4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Lipopolysaccharide biosynthesis protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AYM40_25235 {ECO:0000313|EMBL:ANB75648.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB75648.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB75648.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB75648.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000256|ARBA:ARBA00007430}.
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DR EMBL; CP014579; ANB75648.1; -; Genomic_DNA.
DR RefSeq; WP_063498930.1; NZ_CP014579.1.
DR AlphaFoldDB; A0A160FSP4; -.
DR STRING; 1804984.AYM40_25235; -.
DR KEGG; buz:AYM40_25235; -.
DR Proteomes; UP000076852; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR CDD; cd13127; MATE_tuaB_like; 1.
DR PANTHER; PTHR30250:SF10; LIPOPOLYSACCHARIDE BIOSYNTHESIS PROTEIN WZXC-RELATED; 1.
DR PANTHER; PTHR30250; PST FAMILY PREDICTED COLANIC ACID TRANSPORTER; 1.
DR Pfam; PF13440; Polysacc_synt_3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076852};
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..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..404
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 486 AA; 53171 MW; 8659C890EF008993 CRC64;
MTDNLGRKVL SGLLWSTIQS WGGKLATLAL FAILARLLDS HSFGVFASAM AVLAFVTIFV
DQGLSEAIVQ RPSVTPQLLN TAFFVNLVLS VLVFAVLWVT SPFIAKYMKI LELTNILRAA
SVCVLLTALG FSQQAMQRRN FHYRWLAICS VSSTIVSGVC GTILAFSGYG AWSLVIQILI
NALMNSALLW VRSQWRFSFE FDFAGVRGLF SYGINKLGAQ LLDFGNTRYL EIYLAVNLGA
AALGCYLVGV KIYQALMQAL SGAVLDVAHS GFSRIAHDKD ELARVYYKAI TLTSAVAVPV
FVLLACVAPE VTVIVFGKRW ESSAAIMQPM ALLGAVQALQ FYNGTVYNAL GKPSIGLVFL
VFKTIVTCLA LVLTHGMGLQ SVVWWYAFGQ IITAPPSFIL VQLLVGISLR KIAMRIWPFL
VACAVAAGGV WLIRAGEWIV QWTPFFRLLF LSSTGLLIYS TITILFAKNH IEEVMAVFKG
RRPATS
//
