MOBB_ECOLI
ID MOBB_ECOLI Reviewed; 175 AA.
AC P32125; P76770; Q2M8F4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Molybdopterin-guanine dinucleotide biosynthesis adapter protein;
DE Short=MGD biosynthesis adapter protein;
DE AltName: Full=Molybdenum cofactor biosynthesis adapter protein;
DE Short=Moco biosynthesis adapter protein;
DE AltName: Full=Molybdopterin-guanine dinucleotide biosynthesis protein B;
GN Name=mobB; Synonyms=yihC; OrderedLocusNames=b3856, JW5575;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=7551035; DOI=10.1099/13500872-141-7-1663;
RA Iobbi-Nivol C., Palmer T., Whitty P.W., McNairn E., Boxer D.H.;
RT "The mob locus of Escherichia coli K12 required for molybdenum cofactor
RT biosynthesis is expressed at very low levels.";
RL Microbiology 141:1663-1671(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
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 2-13, GTP-BINDING, GTPASE ACTIVITY, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=9219527; DOI=10.1111/j.1432-1033.1997.t01-1-00690.x;
RA Eaves D.J., Palmer T., Boxer D.H.;
RT "The product of the molybdenum cofactor gene mobB of Escherichia coli is a
RT GTP-binding protein.";
RL Eur. J. Biochem. 246:690-697(1997).
RN [6]
RP NO ROLE IN ACTIVATION OF DMSOR.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10978348; DOI=10.1074/jbc.m007407200;
RA Temple C.A., Rajagopalan K.V.;
RT "Mechanism of assembly of the bis(molybdopterin guanine
RT dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl
RT sulfoxide reductase.";
RL J. Biol. Chem. 275:40202-40210(2000).
RN [7]
RP INTERACTION WITH MOBA; MOGA AND MOEA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12372836; DOI=10.1074/jbc.m205806200;
RA Magalon A., Frixon C., Pommier J., Giordano G., Blasco F.;
RT "In vivo interactions between gene products involved in the final stages of
RT molybdenum cofactor biosynthesis in Escherichia coli.";
RL J. Biol. Chem. 277:48199-48204(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 6-174 IN COMPLEX WITH SULFATE,
RP AND SUBUNIT.
RX PubMed=14646116; DOI=10.1107/s090744490301967x;
RA Rangarajan S.E., Tocilj A., Li Y., Iannuzzi P., Matte A., Cygler M.;
RT "Molecules of Escherichia coli MobB assemble into densely packed hollow
RT cylinders in a crystal lattice with 75% solvent content.";
RL Acta Crystallogr. D 59:2348-2352(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SULFATE, FUNCTION,
RP AND SUBUNIT.
RX PubMed=12682065; DOI=10.1074/jbc.m301485200;
RA McLuskey K., Harrison J.A., Schuttelkopf A.W., Boxer D.H., Hunter W.N.;
RT "Insight into the role of Escherichia coli MobB in molybdenum cofactor
RT biosynthesis based on the high resolution crystal structure.";
RL J. Biol. Chem. 278:23706-23713(2003).
CC -!- FUNCTION: GTP-binding protein that is not required for the biosynthesis
CC of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not
CC necessary for the formation of active molybdoenzymes using this form of
CC molybdenum cofactor. May act as an adapter protein to achieve the
CC efficient biosynthesis and utilization of MGD. Displays a weak
CC intrinsic GTPase activity. Is also able to bind the nucleotides ATP,
CC TTP and GDP, but with lower affinity than GTP.
CC {ECO:0000269|PubMed:12682065, ECO:0000269|PubMed:9219527}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.5 uM for GTP;
CC Note=kcat is 0.003 min(-1) for the GTPase activity.;
CC -!- SUBUNIT: Homodimer. Interacts with MobA, MogA and MoeA in vivo.
CC {ECO:0000269|PubMed:12372836, ECO:0000269|PubMed:12682065,
CC ECO:0000269|PubMed:14646116, ECO:0000269|PubMed:9219527}.
CC -!- INTERACTION:
CC P32125; P30749: moaE; NbExp=2; IntAct=EBI-879965, EBI-554376;
CC -!- INDUCTION: Is expressed at very low levels under both aerobic and
CC anaerobic growth conditions. {ECO:0000269|PubMed:7551035}.
CC -!- SIMILARITY: Belongs to the MobB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB02991.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE77452.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L19201; AAB02991.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76854.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77452.1; ALT_INIT; Genomic_DNA.
DR PIR; S40802; S40802.
DR RefSeq; NP_418293.2; NC_000913.3.
DR RefSeq; WP_000907622.1; NZ_STEB01000017.1.
DR PDB; 1NP6; X-ray; 1.90 A; A/B=2-175.
DR PDB; 1P9N; X-ray; 2.80 A; A/B=6-175.
DR PDBsum; 1NP6; -.
DR PDBsum; 1P9N; -.
DR AlphaFoldDB; P32125; -.
DR SMR; P32125; -.
DR BioGRID; 4262618; 5.
DR BioGRID; 852640; 1.
DR DIP; DIP-10234N; -.
DR IntAct; P32125; 4.
DR STRING; 511145.b3856; -.
DR jPOST; P32125; -.
DR PaxDb; P32125; -.
DR PRIDE; P32125; -.
DR EnsemblBacteria; AAC76854; AAC76854; b3856.
DR EnsemblBacteria; BAE77452; BAE77452; BAE77452.
DR GeneID; 948343; -.
DR KEGG; ecj:JW5575; -.
DR KEGG; eco:b3856; -.
DR PATRIC; fig|1411691.4.peg.2859; -.
DR EchoBASE; EB1775; -.
DR eggNOG; COG1763; Bacteria.
DR HOGENOM; CLU_068199_2_1_6; -.
DR InParanoid; P32125; -.
DR OMA; HTHHNMD; -.
DR PhylomeDB; P32125; -.
DR BioCyc; EcoCyc:EG11828-MON; -.
DR EvolutionaryTrace; P32125; -.
DR PRO; PR:P32125; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005525; F:GTP binding; IDA:EcoCyc.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004435; MobB_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF03205; MobB; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00176; mobB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; GTP-binding;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7551035,
FT ECO:0000269|PubMed:9219527"
FT CHAIN 2..175
FT /note="Molybdopterin-guanine dinucleotide biosynthesis
FT adapter protein"
FT /id="PRO_0000096528"
FT BINDING 17..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305"
FT BINDING 51..54
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 100..103
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:1NP6"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1P9N"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:1NP6"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:1NP6"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:1NP6"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:1NP6"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1NP6"
FT STRAND 73..81
FT /evidence="ECO:0007829|PDB:1NP6"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1NP6"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:1NP6"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1NP6"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1NP6"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:1NP6"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:1NP6"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:1NP6"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:1NP6"
FT HELIX 159..170
FT /evidence="ECO:0007829|PDB:1NP6"
SQ SEQUENCE 175 AA; 19363 MW; 41E0E4EFB2AE160C CRC64;
MAGKTMIPLL AFAAWSGTGK TTLLKKLIPA LCARGIRPGL IKHTHHDMDV DKPGKDSYEL
RKAGAAQTIV ASQQRWALMT ETPDEEELDL QFLASRMDTS KLDLILVEGF KHEEIAKIVL
FRDGAGHRPE ELVIDRHVIA VASDVPLNLD VALLDINDVE GLADFVVEWM QKQNG
