RCSF_ECOL6
ID RCSF_ECOL6 Reviewed; 134 AA.
AC P69412; P28633;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Outer membrane lipoprotein RcsF {ECO:0000255|HAMAP-Rule:MF_00976};
DE Flags: Precursor;
GN Name=rcsF {ECO:0000255|HAMAP-Rule:MF_00976}; OrderedLocusNames=c0237;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Essential component of the Rcs signaling system, which
CC controls transcription of numerous genes. Plays a role in signal
CC transduction from the cell surface to the histidine kinase RcsC. May
CC detect outer membrane defects. {ECO:0000255|HAMAP-Rule:MF_00976}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00976}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_00976};
CC Periplasmic side {ECO:0000255|HAMAP-Rule:MF_00976}.
CC -!- SIMILARITY: Belongs to the RcsF family. {ECO:0000255|HAMAP-
CC Rule:MF_00976}.
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DR EMBL; AE014075; AAN78729.1; -; Genomic_DNA.
DR RefSeq; WP_001202329.1; NC_004431.1.
DR AlphaFoldDB; P69412; -.
DR BMRB; P69412; -.
DR SMR; P69412; -.
DR STRING; 199310.c0237; -.
DR EnsemblBacteria; AAN78729; AAN78729; c0237.
DR GeneID; 67416273; -.
DR KEGG; ecc:c0237; -.
DR eggNOG; ENOG5031XBN; Bacteria.
DR HOGENOM; CLU_142248_1_0_6; -.
DR OMA; FRDMGEV; -.
DR BioCyc; ECOL199310:C0237-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0036406; C:anchored component of periplasmic side of cell outer membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR HAMAP; MF_00976; RcsF; 1.
DR InterPro; IPR030852; RcsF.
DR Pfam; PF16358; RcsF; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Disulfide bond; Lipoprotein; Membrane; Palmitate;
KW Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00976"
FT CHAIN 16..134
FT /note="Outer membrane lipoprotein RcsF"
FT /id="PRO_0000097207"
FT REGION 22..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 16
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00976"
FT LIPID 16
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00976"
FT DISULFID 74..118
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00976"
FT DISULFID 109..124
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00976"
SQ SEQUENCE 134 AA; 14163 MW; 824F82151C07BB41 CRC64;
MRALPICLVA LMLSGCSMLS RSPVEPVQST APQPKAEPAK PKAPRATPVR IYTNAEELVG
KPFRDLGEVS GDSCQASNQD SPPSIPTARK RMQINASKMK ANAVLLHSCE VTSGTPGCYR
QAVCIGSALN ITAK
