CSGG_ECOLI
ID CSGG_ECOLI Reviewed; 277 AA.
AC P0AEA2; P52103;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Curli production assembly/transport component CsgG;
DE Flags: Precursor;
GN Name=csgG; OrderedLocusNames=b1037, JW1020;
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 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8817489; DOI=10.1111/j.1365-2958.1995.mmi_18040661.x.;
RA Hammar M., Arnqvist A., Bian Z., Olsen A., Normark S.;
RT "Expression of two csg operons is required for production of
RT fibronectin- and congo red-binding curli polymers in Escherichia coli K-
RT 12.";
RL Mol. Microbiol. 18:661-670(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
RC STRAIN=O78;
RA Seijffers R., Gophna U., Ron E.Z.;
RT "Avian E. coli serotype O78 csg cluster.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in the biogenesis of curli organelles.
CC -!- INTERACTION:
CC P0AEA2; P0AE95: csgE; NbExp=3; IntAct=EBI-6405292, EBI-16121579;
CC P0AEA2; P0AEA2: csgG; NbExp=4; IntAct=EBI-6405292, EBI-6405292;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: Belongs to the CsgG family. {ECO:0000305}.
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; X90754; CAA62277.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74121.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35818.1; -; Genomic_DNA.
DR EMBL; AF081826; AAD16022.1; -; Genomic_DNA.
DR PIR; S70783; S70783.
DR RefSeq; NP_415555.1; NC_000913.3.
DR RefSeq; WP_001189321.1; NZ_SSUW01000034.1.
DR PDB; 4UV2; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=17-277.
DR PDB; 4UV3; X-ray; 3.59 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=16-277.
DR PDB; 6L7A; EM; 3.38 A; A/B/C/D/E/F/G/H/I=1-277.
DR PDB; 6L7C; EM; 3.34 A; A/B/C/D/E/F/G/H/I=1-277.
DR PDB; 6LQH; EM; 2.94 A; A/B/C/D/E/F/G/H/I=1-277.
DR PDB; 6LQJ; EM; 3.24 A; A/B/C/D/E/F/G/H/I=1-277.
DR PDB; 6SI7; EM; 3.40 A; J/K/L/M/N/O/P/Q/R=16-277.
DR PDB; 7BRM; EM; 3.60 A; A/B/C/D/E/F/G/H/I=1-277.
DR PDBsum; 4UV2; -.
DR PDBsum; 4UV3; -.
DR PDBsum; 6L7A; -.
DR PDBsum; 6L7C; -.
DR PDBsum; 6LQH; -.
DR PDBsum; 6LQJ; -.
DR PDBsum; 6SI7; -.
DR PDBsum; 7BRM; -.
DR AlphaFoldDB; P0AEA2; -.
DR SMR; P0AEA2; -.
DR BioGRID; 4261532; 227.
DR ComplexPortal; CPX-4743; Curli secretion complex.
DR DIP; DIP-9331N; -.
DR IntAct; P0AEA2; 1.
DR STRING; 511145.b1037; -.
DR TCDB; 1.B.48.1.1; the curli fiber subunit porin, cgsa, csgg (csgg) family.
DR PaxDb; P0AEA2; -.
DR PRIDE; P0AEA2; -.
DR EnsemblBacteria; AAC74121; AAC74121; b1037.
DR EnsemblBacteria; BAA35818; BAA35818; BAA35818.
DR GeneID; 66670695; -.
DR GeneID; 945619; -.
DR KEGG; ecj:JW1020; -.
DR KEGG; eco:b1037; -.
DR PATRIC; fig|1411691.4.peg.1234; -.
DR EchoBASE; EB3189; -.
DR eggNOG; COG1462; Bacteria.
DR HOGENOM; CLU_056911_0_0_6; -.
DR InParanoid; P0AEA2; -.
DR OMA; NEPAQLC; -.
DR PhylomeDB; P0AEA2; -.
DR BioCyc; EcoCyc:G6543-MON; -.
DR PRO; PR:P0AEA2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:ComplexPortal.
DR GO; GO:0062155; C:curli secretion complex; IDA:EcoCyc.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0098775; P:curli assembly; IMP:EcoCyc.
DR GO; GO:0098777; P:protein secretion by the type VIII secretion system; IDA:EcoCyc.
DR GO; GO:0071806; P:protein transmembrane transport; IC:ComplexPortal.
DR GO; GO:0044010; P:single-species biofilm formation; IC:ComplexPortal.
DR InterPro; IPR005534; Curli_assmbl/transp-comp_CsgG.
DR Pfam; PF03783; CsgG; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 16..277
FT /note="Curli production assembly/transport component CsgG"
FT /id="PRO_0000021022"
FT LIPID 16
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 16
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:4UV2"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4UV2"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:4UV2"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4UV2"
FT HELIX 79..89
FT /evidence="ECO:0007829|PDB:4UV2"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4UV2"
FT HELIX 101..115
FT /evidence="ECO:0007829|PDB:4UV2"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4UV2"
FT STRAND 135..152
FT /evidence="ECO:0007829|PDB:4UV2"
FT HELIX 153..159
FT /evidence="ECO:0007829|PDB:4UV2"
FT STRAND 165..180
FT /evidence="ECO:0007829|PDB:4UV2"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4UV2"
FT STRAND 185..202
FT /evidence="ECO:0007829|PDB:4UV2"
FT STRAND 205..210
FT /evidence="ECO:0007829|PDB:4UV2"
FT HELIX 212..216
FT /evidence="ECO:0007829|PDB:4UV2"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:4UV2"
FT HELIX 226..248
FT /evidence="ECO:0007829|PDB:4UV2"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:4UV2"
FT HELIX 257..261
FT /evidence="ECO:0007829|PDB:4UV2"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:4UV2"
SQ SEQUENCE 277 AA; 30557 MW; F2DA333BD392F78E CRC64;
MQRLFLLVAV MLLSGCLTAP PKEAARPTLM PRAQSYKDLT HLPAPTGKIF VSVYNIQDET
GQFKPYPASN FSTAVPQSAT AMLVTALKDS RWFIPLERQG LQNLLNERKI IRAAQENGTV
AINNRIPLQS LTAANIMVEG SIIGYESNVK SGGVGARYFG IGADTQYQLD QIAVNLRVVN
VSTGEILSSV NTSKTILSYE VQAGVFRFID YQRLLEGEVG YTSNEPVMLC LMSAIETGVI
FLINDGIDRG LWDLQNKAER QNDILVKYRH MSVPPES
