RFC_SHIDY
ID RFC_SHIDY Reviewed; 380 AA.
AC Q03584;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=O-antigen polymerase;
GN Name=rfc;
OS Shigella dysenteriae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=622;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2469933; DOI=10.1016/0882-4010(86)90056-2;
RA Sturm S., Jann B., Jann K., Fortnagel P., Timmis K.N.;
RT "Genetic and biochemical analysis of Shigella dysenteriae 1 O antigen
RT polysaccharide biosynthesis in Escherichia coli K-12: structure and
RT functions of the rfb gene cluster.";
RL Microb. Pathog. 1:307-324(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7692219; DOI=10.1111/j.1365-2958.1993.tb01700.x;
RA Klena J.D., Schnaitman C.A.;
RT "Function of the rfb gene cluster and the rfe gene in the synthesis of O
RT antigen by Shigella dysenteriae 1.";
RL Mol. Microbiol. 9:393-402(1993).
CC -!- FUNCTION: May link the O-antigen tetrasaccharide units into long
CC chains, giving rise to typical smooth LPS.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
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; L07293; AAA16935.1; -; Unassigned_DNA.
DR PIR; S34964; S34964.
DR AlphaFoldDB; Q03584; -.
DR UniPathway; UPA00030; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Lipopolysaccharide biosynthesis;
KW Membrane; Transmembrane; Transmembrane helix.
FT CHAIN 1..380
FT /note="O-antigen polymerase"
FT /id="PRO_0000097302"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 380 AA; 43732 MW; 557DDC895215E18E CRC64;
MTYFTGFILI LFAIIIKRLT PSQSKKNIVL IANAFWGILL VGYTFNEQYF VPLSATTLFF
ILAFLFFFSM TYILIARSGR VVFSFGTGFI ESKYIYWFAG MINIISICFG IILLYNNHFS
LKVMREGILD GSISGFGLGI SLPLSFCCMY LARHENKKNY FYCFTLLSFL LAVLSTSKIF
LILFLVYIVG INSYVSKKKL LIYGVFVFGL FALSSIILGK FSSDPEGKII SAIFDTLRVY
LFSGLAAFNL YVEKNATLPE NLLLYPFKEV WGTTKDIPKT DILPWINIGV WDTNVYTAFA
PWYQSLGLYA AIIIGILLGF YYGIWFSFRQ NLAVGFYQTF LCFPLLMLFF QEHYLLSWKM
HFIYFLCAIL LAMRKALEYE