RCSF_ECOLI
ID RCSF_ECOLI Reviewed; 134 AA.
AC P69411; P28633;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
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, ECO:0000303|PubMed:1459951};
GN OrderedLocusNames=b0196, JW0192;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1459951; DOI=10.1128/jb.174.24.8016-8022.1992;
RA Gervais F.G., Drapeau G.R.;
RT "Identification, cloning, and characterization of rcsF, a new regulator
RT gene for exopolysaccharide synthesis that suppresses the division mutation
RT ftsZ84 in Escherichia coli K-12.";
RL J. Bacteriol. 174:8016-8022(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Miyamoto K.;
RL Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 37-38 AND 46.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP FUNCTION.
RC STRAIN=K12 / ST001;
RX PubMed=13129944; DOI=10.1128/jb.185.19.5735-5746.2003;
RA Hagiwara D., Sugiura M., Oshima T., Mori H., Aiba H., Yamashino T.,
RA Mizuno T.;
RT "Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB
RT phosphorelay system in Escherichia coli.";
RL J. Bacteriol. 185:5735-5746(2003).
RN [8]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=14651646; DOI=10.1046/j.1365-2958.2003.03815.x;
RA Ferrieres L., Clarke D.J.;
RT "The RcsC sensor kinase is required for normal biofilm formation in
RT Escherichia coli K-12 and controls the expression of a regulon in response
RT to growth on a solid surface.";
RL Mol. Microbiol. 50:1665-1682(2003).
RN [9]
RP FUNCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16166540; DOI=10.1128/jb.187.19.6770-6778.2005;
RA Majdalani N., Heck M., Stout V., Gottesman S.;
RT "Role of RcsF in signaling to the Rcs phosphorelay pathway in Escherichia
RT coli.";
RL J. Bacteriol. 187:6770-6778(2005).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16740933; DOI=10.1128/jb.00004-06;
RA Castanie-Cornet M.P., Cam K., Jacq A.;
RT "RcsF is an outer membrane lipoprotein involved in the RcsCDB phosphorelay
RT signaling pathway in Escherichia coli.";
RL J. Bacteriol. 188:4264-4270(2006).
RN [11]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=23813676; DOI=10.1099/mic.0.069328-0;
RA Umekawa M., Miyagawa H., Kondo D., Matsuoka S., Matsumoto K., Hara H.;
RT "Importance of the proline-rich region for the regulatory function of RcsF,
RT an outer membrane lipoprotein component of the Escherichia coli Rcs signal
RT transduction system.";
RL Microbiology 159:1818-1827(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 17-134, INTERACTION WITH DSBC,
RP DISULFIDE BONDS, AND MUTAGENESIS OF CYS-74; CYS-109; CYS-118 AND CYS-124.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=21454485; DOI=10.1074/jbc.m111.224865;
RA Leverrier P., Declercq J.P., Denoncin K., Vertommen D., Hiniker A.,
RA Cho S.H., Collet J.F.;
RT "Crystal structure of the outer membrane protein RcsF, a new substrate for
RT the periplasmic protein-disulfide isomerase DsbC.";
RL J. Biol. Chem. 286:16734-16742(2011).
RN [13]
RP STRUCTURE BY NMR OF 31-134, DISULFIDE BONDS, AND MUTAGENESIS OF CYS-7;
RP CYS-16; CYS-74; ARG-89; LYS-90; CYS-109; CYS-118 AND CYS-124.
RX PubMed=21471196; DOI=10.1074/jbc.m111.230185;
RA Rogov V.V., Rogova N.Y., Bernhard F., Lohr F., Dotsch V.;
RT "A disulfide bridge network within the soluble periplasmic domain
RT determines structure and function of the outer membrane protein RcsF.";
RL J. Biol. Chem. 286:18775-18783(2011).
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. The system controls expression of genes
CC involved in colanic acid capsule synthesis, biofilm formation and cell
CC division. {ECO:0000255|HAMAP-Rule:MF_00976,
CC ECO:0000269|PubMed:13129944, ECO:0000269|PubMed:14651646,
CC ECO:0000269|PubMed:16166540, ECO:0000269|PubMed:16740933}.
CC -!- SUBUNIT: Interacts with DsbC. {ECO:0000269|PubMed:21454485}.
CC -!- INTERACTION:
CC P69411; P0A940: bamA; NbExp=3; IntAct=EBI-1114706, EBI-907371;
CC P69411; P0A910: ompA; NbExp=3; IntAct=EBI-1114706, EBI-371347;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_00976, ECO:0000269|PubMed:16740933,
CC ECO:0000269|PubMed:23813676}; Lipid-anchor {ECO:0000255|HAMAP-
CC Rule:MF_00976, ECO:0000269|PubMed:16740933,
CC ECO:0000269|PubMed:23813676}; Periplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_00976, ECO:0000269|PubMed:16740933,
CC ECO:0000269|PubMed:23813676}.
CC -!- DOMAIN: Contains an N-terminal proline-rich region (PRR), which
CC probably plays an important role in the regulation of function of RcsF
CC and activation of the Rcs signaling system.
CC {ECO:0000269|PubMed:23813676}.
CC -!- MISCELLANEOUS: The formation of the non-consecutive disulfides depends
CC on the periplasmic disulfide isomerase DsbC. The disulfide bond between
CC Cys-109 and Cys-124 is particularly important for the assembly of an
CC active RcsF (PubMed:21454485). {ECO:0000305|PubMed:21454485}.
CC -!- SIMILARITY: Belongs to the RcsF family. {ECO:0000255|HAMAP-
CC Rule:MF_00976}.
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DR EMBL; L04474; AAA24508.1; -; Genomic_DNA.
DR EMBL; D15061; BAA03656.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08624.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73307.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77873.2; -; Genomic_DNA.
DR PIR; D64744; D64744.
DR RefSeq; NP_414738.1; NC_000913.3.
DR RefSeq; WP_001202329.1; NZ_STEB01000032.1.
DR PDB; 2L8Y; NMR; -; A=31-134.
DR PDB; 2Y1B; X-ray; 2.00 A; A=17-134.
DR PDB; 6T1W; X-ray; 3.79 A; C/D=1-134.
DR PDBsum; 2L8Y; -.
DR PDBsum; 2Y1B; -.
DR PDBsum; 6T1W; -.
DR AlphaFoldDB; P69411; -.
DR BMRB; P69411; -.
DR SMR; P69411; -.
DR BioGRID; 4259530; 12.
DR IntAct; P69411; 10.
DR STRING; 511145.b0196; -.
DR jPOST; P69411; -.
DR PaxDb; P69411; -.
DR PRIDE; P69411; -.
DR EnsemblBacteria; AAC73307; AAC73307; b0196.
DR EnsemblBacteria; BAA77873; BAA77873; BAA77873.
DR GeneID; 67416273; -.
DR GeneID; 949113; -.
DR KEGG; ecj:JW0192; -.
DR KEGG; eco:b0196; -.
DR PATRIC; fig|1411691.4.peg.2082; -.
DR EchoBASE; EB1465; -.
DR eggNOG; ENOG5031XBN; Bacteria.
DR HOGENOM; CLU_142248_1_0_6; -.
DR InParanoid; P69411; -.
DR OMA; FRDMGEV; -.
DR PhylomeDB; P69411; -.
DR BioCyc; EcoCyc:RCSF-MON; -.
DR PRO; PR:P69411; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0036406; C:anchored component of periplasmic side of cell outer membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0106234; C:outer membrane protein complex; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0036460; P:cellular response to cell envelope stress; IDA:EcoCyc.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0070299; P:positive regulation of phosphorelay signal transduction system; IDA:EcoCyc.
DR HAMAP; MF_00976; RcsF; 1.
DR InterPro; IPR030852; RcsF.
DR Pfam; PF16358; RcsF; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsule biogenesis/degradation; Cell outer membrane;
KW Disulfide bond; Lipoprotein; Membrane; Palmitate; Reference proteome;
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_0000097208"
FT REGION 22..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..50
FT /note="PRR"
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 ECO:0000269|PubMed:21454485, ECO:0000269|PubMed:21471196"
FT DISULFID 109..124
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00976,
FT ECO:0000269|PubMed:21454485, ECO:0000269|PubMed:21471196"
FT MUTAGEN 7
FT /note="C->S: Does not affect exopolysaccharide
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:21471196"
FT MUTAGEN 16
FT /note="C->S: Strongly decreases exopolysaccharide
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:21471196"
FT MUTAGEN 74
FT /note="C->S: Mucoid phenotype. Decreases exopolysaccharide
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:21454485,
FT ECO:0000269|PubMed:21471196"
FT MUTAGEN 89
FT /note="R->A: Does not affect exopolysaccharide
FT biosynthesis; when associated with A-90."
FT /evidence="ECO:0000269|PubMed:21471196"
FT MUTAGEN 90
FT /note="K->A: Does not affect exopolysaccharide
FT biosynthesis; when associated with A-89."
FT /evidence="ECO:0000269|PubMed:21471196"
FT MUTAGEN 109
FT /note="C->S: Does not activate the production of capsule
FT polysaccharides."
FT /evidence="ECO:0000269|PubMed:21454485,
FT ECO:0000269|PubMed:21471196"
FT MUTAGEN 118
FT /note="C->S: Mucoid phenotype. Decreases exopolysaccharide
FT biosynthesis."
FT /evidence="ECO:0000269|PubMed:21454485,
FT ECO:0000269|PubMed:21471196"
FT MUTAGEN 124
FT /note="C->S: Does not activate the production of capsule
FT polysaccharides."
FT /evidence="ECO:0000269|PubMed:21454485,
FT ECO:0000269|PubMed:21471196"
FT CONFLICT 37..38
FT /note="EP -> DA (in Ref. 1; AAA24508)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="Missing (in Ref. 1; AAA24508)"
FT /evidence="ECO:0000305"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2Y1B"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:2Y1B"
FT STRAND 63..75
FT /evidence="ECO:0007829|PDB:2Y1B"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:2Y1B"
FT STRAND 102..113
FT /evidence="ECO:0007829|PDB:2Y1B"
FT STRAND 119..131
FT /evidence="ECO:0007829|PDB:2Y1B"
SQ SEQUENCE 134 AA; 14163 MW; 824F82151C07BB41 CRC64;
MRALPICLVA LMLSGCSMLS RSPVEPVQST APQPKAEPAK PKAPRATPVR IYTNAEELVG
KPFRDLGEVS GDSCQASNQD SPPSIPTARK RMQINASKMK ANAVLLHSCE VTSGTPGCYR
QAVCIGSALN ITAK
