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MOBB_BACSU
ID   MOBB_BACSU              Reviewed;         173 AA.
AC   O31704;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Probable 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;
GN   Name=mobB; OrderedLocusNames=BSU14290;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Caldwell R.M., Ferrari E.;
RT   "Sequence analysis of the mobA-ampS region of the Bacillus subtilis
RT   chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MobB family. {ECO:0000305}.
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DR   EMBL; AF012285; AAC24903.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13302.1; -; Genomic_DNA.
DR   PIR; D69659; D69659.
DR   RefSeq; NP_389312.1; NC_000964.3.
DR   RefSeq; WP_003232370.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O31704; -.
DR   SMR; O31704; -.
DR   STRING; 224308.BSU14290; -.
DR   PaxDb; O31704; -.
DR   PRIDE; O31704; -.
DR   EnsemblBacteria; CAB13302; CAB13302; BSU_14290.
DR   GeneID; 938790; -.
DR   KEGG; bsu:BSU14290; -.
DR   PATRIC; fig|224308.179.peg.1559; -.
DR   eggNOG; COG1763; Bacteria.
DR   InParanoid; O31704; -.
DR   OMA; YKHRQAG; -.
DR   PhylomeDB; O31704; -.
DR   BioCyc; BSUB:BSU14290-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   GTP-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..173
FT                   /note="Probable molybdopterin-guanine dinucleotide
FT                   biosynthesis adapter protein"
FT                   /id="PRO_0000096527"
FT   BINDING         17..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         51..56
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   BINDING         99..101
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   173 AA;  19145 MW;  8F46203BAEA2B8C8 CRC64;
     MALVRPFPIV QVVGFQNSGK TTFIERILEK ASEQGVHLGC LKHHGHGGEP QTLTEGKDTD
     RYKAAGADVT AVEGAGVLQL TARRNWDLAR LIELYQFLET DCLLIEGFKK APYPKVVILS
     EKEDLEALQA VNIIAIIYRK KEHMTEHQGL PVFHADDPVA VDFVLSQLKG ESA
 
 
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