CUSF_ECOLI
ID CUSF_ECOLI Reviewed; 110 AA.
AC P77214;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Cation efflux system protein CusF;
DE Flags: Precursor;
GN Name=cusF; Synonyms=cusX, ylcC; OrderedLocusNames=b0573, JW0562;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [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 PROTEIN SEQUENCE OF 22-26, CHARACTERIZATION, AND MUTAGENESIS OF
RP 25-HIS--HIS-27; ASP-48; 57-HIS-HIS-58; MET-69; MET-71 AND PHE-73.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=12813074; DOI=10.1128/jb.185.13.3804-3812.2003;
RA Franke S., Grass G., Rensing C., Nies D.H.;
RT "Molecular analysis of the copper-transporting efflux system CusCFBA of
RT Escherichia coli.";
RL J. Bacteriol. 185:3804-3812(2003).
RN [6]
RP FUNCTION IN COPPER HOMEOSTASIS.
RC STRAIN=K12;
RX PubMed=11399769; DOI=10.1074/jbc.m104122200;
RA Outten F.W., Huffman D.L., Hale J.A., O'Halloran T.V.;
RT "The independent cue and cus systems confer copper tolerance during aerobic
RT and anaerobic growth in Escherichia coli.";
RL J. Biol. Chem. 276:30670-30677(2001).
RN [7]
RP INDUCTION.
RC STRAIN=K38;
RX PubMed=11283292; DOI=10.1099/00221287-147-4-965;
RA Franke S., Grass G., Nies D.H.;
RT "The product of the ybdE gene of the Escherichia coli chromosome is
RT involved in detoxification of silver ions.";
RL Microbiology 147:965-972(2001).
RN [8]
RP FUNCTION, COPPER-BINDING, SUBUNIT, AND MUTAGENESIS OF 69-MET--MET-71.
RX PubMed=24917681; DOI=10.1074/jbc.m114.577668;
RA Padilla-Benavides T., George Thompson A.M., McEvoy M.M., Argueello J.M.;
RT "Mechanism of ATPase-mediated Cu+ export and delivery to periplasmic
RT chaperones: the interaction of Escherichia coli CopA and CusF.";
RL J. Biol. Chem. 289:20492-20501(2014).
CC -!- FUNCTION: Part of a cation efflux system that mediates resistance to
CC copper and silver. Binds one copper per polypeptide (PubMed:11399769,
CC PubMed:24917681). {ECO:0000269|PubMed:11399769,
CC ECO:0000269|PubMed:24917681}.
CC -!- SUBUNIT: The cus efflux system is composed of CusA, CusB, CusC and
CC CusF. Interacts with copper-exporting P-type ATPase CopA; when this
CC protein is precharged with copper it binds very little CopA
CC (PubMed:24917681). {ECO:0000305|PubMed:24917681}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: Transcriptionally regulated by CusR in response to copper
CC and silver ions. {ECO:0000269|PubMed:11283292}.
CC -!- MISCELLANEOUS: The cus system plays an important role in copper
CC tolerance under anaerobic growth and, under extreme copper stress, in
CC aerobic growth.
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DR EMBL; U82598; AAB40771.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73674.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35207.1; -; Genomic_DNA.
DR PIR; C64790; C64790.
DR RefSeq; NP_415105.1; NC_000913.3.
DR RefSeq; WP_000709870.1; NZ_SSZK01000024.1.
DR PDB; 1ZEQ; X-ray; 1.50 A; X=28-110.
DR PDB; 2QCP; X-ray; 1.00 A; X=32-110.
DR PDB; 2VB2; X-ray; 1.70 A; X=23-110.
DR PDB; 2VB3; X-ray; 2.33 A; X=23-110.
DR PDB; 3E6Z; X-ray; 1.00 A; X=32-110.
DR PDBsum; 1ZEQ; -.
DR PDBsum; 2QCP; -.
DR PDBsum; 2VB2; -.
DR PDBsum; 2VB3; -.
DR PDBsum; 3E6Z; -.
DR AlphaFoldDB; P77214; -.
DR SMR; P77214; -.
DR BioGRID; 4262045; 218.
DR ComplexPortal; CPX-2254; Cus cation efflux complex.
DR DIP; DIP-9350N; -.
DR IntAct; P77214; 2.
DR STRING; 511145.b0573; -.
DR TCDB; 2.A.6.1.4; the resistance-nodulation-cell division (rnd) superfamily.
DR PaxDb; P77214; -.
DR PRIDE; P77214; -.
DR EnsemblBacteria; AAC73674; AAC73674; b0573.
DR EnsemblBacteria; BAA35207; BAA35207; BAA35207.
DR GeneID; 945188; -.
DR KEGG; ecj:JW0562; -.
DR KEGG; eco:b0573; -.
DR PATRIC; fig|1411691.4.peg.1701; -.
DR EchoBASE; EB3985; -.
DR eggNOG; COG5569; Bacteria.
DR HOGENOM; CLU_140852_2_1_6; -.
DR InParanoid; P77214; -.
DR OMA; MHEQPAA; -.
DR BioCyc; EcoCyc:G6321-MON; -.
DR BioCyc; MetaCyc:G6321-MON; -.
DR EvolutionaryTrace; P77214; -.
DR PRO; PR:P77214; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IMP:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IMP:EcoliWiki.
DR GO; GO:0016531; F:copper chaperone activity; IDA:EcoCyc.
DR GO; GO:0005507; F:copper ion binding; IDA:EcoCyc.
DR GO; GO:0016530; F:metallochaperone activity; IDA:EcoliWiki.
DR GO; GO:0046914; F:transition metal ion binding; IDA:EcoCyc.
DR GO; GO:0060003; P:copper ion export; IC:ComplexPortal.
DR GO; GO:0035434; P:copper ion transmembrane transport; IC:ComplexPortal.
DR GO; GO:0046688; P:response to copper ion; IEP:EcoCyc.
DR GO; GO:0010272; P:response to silver ion; IMP:EcoCyc.
DR GO; GO:0009636; P:response to toxic substance; IC:ComplexPortal.
DR GO; GO:0010043; P:response to zinc ion; IEP:EcoCyc.
DR GO; GO:1902601; P:silver ion transmembrane transport; IC:ComplexPortal.
DR Gene3D; 2.40.50.320; -; 1.
DR InterPro; IPR021647; CusF_Ec.
DR InterPro; IPR042230; CusF_sf.
DR Pfam; PF11604; CusF_Ec; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Metal-binding; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:12813074"
FT CHAIN 22..110
FT /note="Cation efflux system protein CusF"
FT /id="PRO_0000021046"
FT MUTAGEN 25..27
FT /note="HHH->QQQ: No change in copper resistance."
FT /evidence="ECO:0000269|PubMed:12813074"
FT MUTAGEN 45..57
FT /note="KGIDLESKKITIH->AGIDLESAAITIA: Wild-type Cu(+)
FT binding, 50% decrease in Cu transfer from CopA; when
FT associated with A-72."
FT /evidence="ECO:0000269|PubMed:24917681"
FT MUTAGEN 48
FT /note="D->N: No change in copper resistance."
FT /evidence="ECO:0000269|PubMed:12813074"
FT MUTAGEN 57..58
FT /note="HH->QQ: Slight decrease in copper resistance."
FT /evidence="ECO:0000269|PubMed:12813074"
FT MUTAGEN 69..71
FT /note="MTM->ITI: Binds Cu(+) very poorly, does not receive
FT Cu(+) from CopA."
FT /evidence="ECO:0000269|PubMed:24917681"
FT MUTAGEN 69
FT /note="M->I: Loss of copper resistance and strong decrease
FT in copper binding; when associated with I-71."
FT /evidence="ECO:0000269|PubMed:12813074"
FT MUTAGEN 71
FT /note="M->I: Loss of copper resistance and strong decrease
FT in copper binding; when associated with I-69."
FT /evidence="ECO:0000269|PubMed:12813074"
FT MUTAGEN 72
FT /note="R->A: Wild-type Cu(+) binding, 50% decrease in Cu
FT transfer from CopA; when associated with 45-A--A-57."
FT /evidence="ECO:0000269|PubMed:24917681"
FT MUTAGEN 73
FT /note="F->Y: No change in copper resistance."
FT /evidence="ECO:0000269|PubMed:12813074"
FT STRAND 38..48
FT /evidence="ECO:0007829|PDB:2QCP"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:2QCP"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:2QCP"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:2QCP"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:2QCP"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:2VB3"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:2QCP"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:2QCP"
SQ SEQUENCE 110 AA; 12251 MW; 494011382E05DB59 CRC64;
MKKALQVAMF SLFTVIGFNA QANEHHHETM SEAQPQVISA TGVVKGIDLE SKKITIHHDP
IAAVNWPEMT MRFTITPQTK MSEIKTGDKV AFNFVQQGNL SLLQDIKVSQ
