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DNAB_BACSU
ID   DNAB_BACSU              Reviewed;         472 AA.
AC   P07908;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Replication initiation and membrane attachment protein;
GN   Name=dnaB; OrderedLocusNames=BSU28990;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANTS DNABI AND DNABII.
RC   STRAIN=168 / PY79;
RX   PubMed=3027697; DOI=10.1073/pnas.84.3.653;
RA   Hoshino T., McKenzie T., Schmidt S., Tanaka T., Sueoka N.;
RT   "Nucleotide sequence of Bacillus subtilis dnaB: a gene essential for DNA
RT   replication initiation and membrane attachment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:653-657(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3027671; DOI=10.1093/nar/14.24.9989;
RA   Ogasawara N., Moriya S., Mazza P.G., Yoshikawa H.;
RT   "Nucleotide sequence and organization of dnaB gene and neighbouring genes
RT   on the Bacillus subtilis chromosome.";
RL   Nucleic Acids Res. 14:9989-9999(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969504; DOI=10.1099/13500872-142-11-3067;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis
RT   chromosome containing genes responsible for stress responses, the
RT   utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [5]
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: Probable component of primosome involved in the initiation of
CC       DNA replication. It is essential for both replication initiation and
CC       membrane attachment of the origin region of the chromosome and plasmid
CC       pUB110.
CC   -!- MISCELLANEOUS: The two mutants dna-1 (dnaBI) and dnaB-19 (dnaBII) show
CC       different characteristics for replication and membrane binding of
CC       plasmid pUB110. DnaBI is essential for both chromosome and pUB110
CC       replication, whereas dnaBII is necessary only for chromosome
CC       replication.
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DR   EMBL; M15183; AAA22404.1; -; Genomic_DNA.
DR   EMBL; X04963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z75208; CAA99604.1; -; Genomic_DNA.
DR   EMBL; AF008220; AAC00358.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14859.1; -; Genomic_DNA.
DR   PIR; B26580; B26580.
DR   RefSeq; NP_390777.1; NC_000964.3.
DR   RefSeq; WP_003229464.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P07908; -.
DR   SMR; P07908; -.
DR   IntAct; P07908; 4.
DR   STRING; 224308.BSU28990; -.
DR   PaxDb; P07908; -.
DR   EnsemblBacteria; CAB14859; CAB14859; BSU_28990.
DR   GeneID; 937396; -.
DR   KEGG; bsu:BSU28990; -.
DR   PATRIC; fig|224308.179.peg.3148; -.
DR   eggNOG; COG3611; Bacteria.
DR   OMA; KIASHWA; -.
DR   PhylomeDB; P07908; -.
DR   BioCyc; BSUB:BSU28990-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.630; -; 1.
DR   InterPro; IPR034829; DnaD-like_sf.
DR   InterPro; IPR006343; DnaD_dom.
DR   Pfam; PF07261; DnaB_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA replication; DNA-binding; Nucleotide-binding; Primosome;
KW   Reference proteome.
FT   CHAIN           1..472
FT                   /note="Replication initiation and membrane attachment
FT                   protein"
FT                   /id="PRO_0000079950"
FT   DNA_BIND        80..99
FT                   /evidence="ECO:0000305"
FT   REGION          415..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         122..143
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   BINDING         398..419
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         113
FT                   /note="P->L: In DnaBI; required for chromosome and plasmid
FT                   replication."
FT   MUTAGEN         379
FT                   /note="A->T: In DnaBII; required only for chromosome
FT                   replication."
SQ   SEQUENCE   472 AA;  54890 MW;  8BDC5B2F6C67DB2E CRC64;
     MADYWKDVLP VDPYVVKSRS MLQDIDRQII TQLYQPLIGP VAFSLYMTLW GELEQNRLWG
     GESTHRQLMG MTQSNLKTIH QEQGKLEGIG LLKVYMKESE RQERLFIYEL LPPLRPNEFF
     EDGMLNVFLY NRVGKTKYQQ LKQFFTHPAI SEDAKDITRP FNHAFESLQP SEWKLTSDME
     ETVRLAEGSE YTSVGQSPSY TITEDVFDFD LFLAGLSETM IPRKAMTQQV RDTIKKLSYL
     YGIDPLQMQN VVMSAIDERD VITTEALRKA ASDWYQIERN GQLPDLVEKT QPVHLREGEQ
     PAEEDSLDGK LIALLEAISP KKLLQDIADG TEPSKADLKI IEEIMFEQKL EPGVTNVLIY
     YVMLKTDMKL SKNYIQKIAS HWARKKVKTV REAMKLAIEE NRQYLEWAEG KTKSSKRNQK
     VIREEKLPDW MTEKETASDS ESGQQKLHPQ DLEEQKKKMM EEMQKLKKYS AY
 
 
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