MODF_ECOLI
ID MODF_ECOLI Reviewed; 490 AA.
AC P31060;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=ABC transporter ATP-binding protein ModF;
DE AltName: Full=Photorepair protein PhrA {ECO:0000303|PubMed:8310005};
GN Name=modF;
GN Synonyms=ORF6 {ECO:0000303|PubMed:8564363},
GN phrA {ECO:0000303|PubMed:8310005}; OrderedLocusNames=b0760, JW0743;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=8564363; DOI=10.1016/s0944-5013(11)80016-9;
RA Walkenhorst H.M., Hemschemeier S.K., Eichenlaub R.;
RT "Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia
RT coli and modR, a regulatory gene.";
RL Microbiol. Res. 150:347-361(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISCUSSION OF SEQUENCE.
RC STRAIN=K12 / BW545;
RX PubMed=8550508; DOI=10.1128/jb.178.3.735-744.1996;
RA Grunden A.M., Ray R.M., Rosentel J.K., Healy F.G., Shanmugam K.T.;
RT "Repression of the Escherichia coli modABCD (molybdate transport) operon by
RT ModE.";
RL J. Bacteriol. 178:735-744(1996).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 151-490.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=8310005; DOI=10.1111/j.1751-1097.1993.tb04979.x;
RA Dorrell N., Ahmed A.H., Moss S.H.;
RT "Photoreactivation in a phrB mutant of Escherichia coli K-12: evidence for
RT the role of a second protein in photorepair.";
RL Photochem. Photobiol. 58:831-835(1993).
CC -!- FUNCTION: Probably not involved in the transport of molybdenum into the
CC cell. {ECO:0000269|PubMed:8564363}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: Probably part of the modE-modF operon.
CC {ECO:0000305|PubMed:8564363}.
CC -!- DISRUPTION PHENOTYPE: Not required for synthesis of the molybdenum
CC cofactor or for the uptake of molybdate (PubMed:8564363).
CC {ECO:0000269|PubMed:8564363}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be PhrA, involved in
CC photoreactivation. The protein was thought to be the C-terminus of what
CC is now accepted to be a longer reading frame called ModF;
CC overexpression from a plasmid yields an approximately 50 kDa protein,
CC which is too long to be PhrA (PubMed:8564363).
CC {ECO:0000269|PubMed:8564363, ECO:0000305|PubMed:8310005,
CC ECO:0000305|PubMed:8550508}.
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DR EMBL; U07867; AAB06891.1; -; Genomic_DNA.
DR EMBL; U27192; AAB60176.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73847.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35422.1; -; Genomic_DNA.
DR EMBL; X69182; CAA48926.1; -; Genomic_DNA.
DR PIR; JC6038; JC6038.
DR RefSeq; NP_415281.1; NC_000913.3.
DR RefSeq; WP_000096869.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P31060; -.
DR SMR; P31060; -.
DR BioGRID; 4263124; 95.
DR BioGRID; 849744; 1.
DR IntAct; P31060; 7.
DR STRING; 511145.b0760; -.
DR jPOST; P31060; -.
DR PaxDb; P31060; -.
DR PRIDE; P31060; -.
DR EnsemblBacteria; AAC73847; AAC73847; b0760.
DR EnsemblBacteria; BAA35422; BAA35422; BAA35422.
DR GeneID; 945368; -.
DR KEGG; ecj:JW0743; -.
DR KEGG; eco:b0760; -.
DR PATRIC; fig|1411691.4.peg.1518; -.
DR EchoBASE; EB1628; -.
DR eggNOG; COG1119; Bacteria.
DR HOGENOM; CLU_000604_45_0_6; -.
DR InParanoid; P31060; -.
DR OMA; TIWDIKQ; -.
DR PhylomeDB; P31060; -.
DR BioCyc; EcoCyc:MODF-MON; -.
DR PRO; PR:P31060; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell inner membrane; Cell membrane; DNA damage; DNA repair;
KW Membrane; Nucleotide-binding; Reference proteome; Repeat; Transport.
FT CHAIN 1..490
FT /note="ABC transporter ATP-binding protein ModF"
FT /id="PRO_0000092566"
FT DOMAIN 4..235
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 261..489
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 293..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 320
FT /note="L -> A (in Ref. 6; CAA48926)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="G -> R (in Ref. 6; CAA48926)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="R -> A (in Ref. 6; CAA48926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 54536 MW; 97C220824ED66FB3 CRC64;
MSSLQILQGT FRLSDTKTLQ LPQLTLNAGD SWAFVGSNGS GKSALARALA GELPLLKGER
QSQFSHITRL SFEQLQKLVS DEWQRNNTDM LGPGEDDTGR TTAEIIQDEV KDAPRCMQLA
QQFGITALLD RRFKYLSTGE TRKTLLCQAL MSEPDLLILD EPFDGLDVAS RQQLAERLAS
LHQSGITLVL VLNRFDEIPE FVQFAGVLAD CTLAETGAKE ELLQQALVAQ LAHSEQLEGV
QLPEPDEPSA RHALPANEPR IVLNNGVVSY NDRPILNNLS WQVNPGEHWQ IVGPNGAGKS
TLLSLVTGDH PQGYSNDLTL FGRRRGSGET IWDIKKHIGY VSSSLHLDYR VSTTVRNVIL
SGYFDSIGIY QAVSDRQQKL VQQWLDILGI DKRTADAPFH SLSWGQQRLA LIVRALVKHP
TLLILDEPLQ GLDPLNRQLI RRFVDVLISE GETQLLFVSH HAEDAPACIT HRLEFVPDGG
LYRYVLTKIY
