MODB_ECOLI
ID MODB_ECOLI Reviewed; 229 AA.
AC P0AF01; P09834; P77537;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Molybdenum transport system permease protein ModB;
GN Name=modB; Synonyms=chlJ; OrderedLocusNames=b0764, JW0747;
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=7665460; DOI=10.1128/jb.177.17.4851-4856.1995;
RA Maupin-Furlow J.A., Rosentel J.K., Lee J.H., Deppenmeier U., Gunsalus R.P.,
RA Shanmugam K.T.;
RT "Genetic analysis of the modABCD (molybdate transport) operon of
RT Escherichia coli.";
RL J. Bacteriol. 177:4851-4856(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [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 30-229.
RC STRAIN=K12;
RX PubMed=3553151; DOI=10.1128/jb.169.5.1911-1916.1987;
RA Johann S., Hinton S.M.;
RT "Cloning and nucleotide sequence of the chlD locus.";
RL J. Bacteriol. 169:1911-1916(1987).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Part of the binding-protein-dependent transport system for
CC molybdenum; probably responsible for the translocation of the substrate
CC across the membrane.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
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DR EMBL; L34009; AAB00836.1; -; Genomic_DNA.
DR EMBL; U27192; AAB60172.1; -; Genomic_DNA.
DR EMBL; U07867; AAB06894.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73851.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35428.1; -; Genomic_DNA.
DR EMBL; M16182; AAA83839.1; -; Genomic_DNA.
DR PIR; D64812; BVECHJ.
DR RefSeq; NP_415285.1; NC_000913.3.
DR RefSeq; WP_000604034.1; NZ_STEB01000028.1.
DR AlphaFoldDB; P0AF01; -.
DR SMR; P0AF01; -.
DR BioGRID; 4261270; 8.
DR ComplexPortal; CPX-4342; Molybdate ABC transporter complex.
DR IntAct; P0AF01; 4.
DR STRING; 511145.b0764; -.
DR TCDB; 3.A.1.8.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; P0AF01; -.
DR PRIDE; P0AF01; -.
DR EnsemblBacteria; AAC73851; AAC73851; b0764.
DR EnsemblBacteria; BAA35428; BAA35428; BAA35428.
DR GeneID; 67413803; -.
DR GeneID; 945361; -.
DR KEGG; ecj:JW0747; -.
DR KEGG; eco:b0764; -.
DR PATRIC; fig|1411691.4.peg.1514; -.
DR EchoBASE; EB0002; -.
DR eggNOG; COG4149; Bacteria.
DR HOGENOM; CLU_016047_14_3_6; -.
DR InParanoid; P0AF01; -.
DR OMA; MYSFIET; -.
DR PhylomeDB; P0AF01; -.
DR BioCyc; EcoCyc:MODB-MON; -.
DR BioCyc; MetaCyc:MODB-MON; -.
DR PRO; PR:P0AF01; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015098; F:molybdate ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015689; P:molybdate ion transport; IC:ComplexPortal.
DR GO; GO:0070614; P:tungstate ion transport; IC:ComplexPortal.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR InterPro; IPR011867; ModB_ABC.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR02141; modB_ABC; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Molybdenum;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..229
FT /note="Molybdenum transport system permease protein ModB"
FT /id="PRO_0000060111"
FT TOPO_DOM 1..16
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 38..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 71..83
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 105..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 158..201
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 223..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 11..219
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT CONFLICT 40
FT /note="T -> S (in Ref. 1, 2 and 6)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 24939 MW; 65A3A05FBF3382C6 CRC64;
MILTDPEWQA VLLSLKVSSL AVLFSLPFGI FFAWLLVRCT FPGKALLDSV LHLPLVLPPV
VVGYLLLVSM GRRGFIGERL YDWFGITFAF SWRGAVLAAA VMSFPLMVRA IRLALEGVDV
KLEQAARTLG AGRWRVFFTI TLPLTLPGII VGTVLAFARS LGEFGATITF VSNIPGETRT
IPSAMYTLIQ TPGGESGAAR LCIISIALAM ISLLISEWLA RISRERAGR
