DNAB_MYCGE
ID DNAB_MYCGE Reviewed; 468 AA.
AC P47340; Q49285; Q49456;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Replicative DNA helicase;
DE EC=3.6.4.12;
GN Name=dnaB; OrderedLocusNames=MG094;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98 AND 267-378.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
RN [3]
RP SEQUENCE REVISION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=16407165; DOI=10.1073/pnas.0510013103;
RA Glass J.I., Assad-Garcia N., Alperovich N., Yooseph S., Lewis M.R.,
RA Maruf M., Hutchison C.A. III, Smith H.O., Venter J.C.;
RT "Essential genes of a minimal bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:425-430(2006).
CC -!- FUNCTION: Participates in initiation and elongation during chromosome
CC replication; it exhibits DNA-dependent ATPase activity. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- DISRUPTION PHENOTYPE: Probably essential, it was not disrupted in a
CC global transposon mutagenesis study. {ECO:0000269|PubMed:16407165}.
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD12440.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L43967; AAC71312.2; -; Genomic_DNA.
DR EMBL; U02158; AAD12440.1; ALT_INIT; Genomic_DNA.
DR EMBL; U01803; AAD12329.1; -; Genomic_DNA.
DR RefSeq; WP_010869329.1; NC_000908.2.
DR AlphaFoldDB; P47340; -.
DR SMR; P47340; -.
DR STRING; 243273.MG_094; -.
DR EnsemblBacteria; AAC71312; AAC71312; MG_094.
DR KEGG; mge:MG_094; -.
DR eggNOG; COG0305; Bacteria.
DR HOGENOM; CLU_005373_0_0_14; -.
DR OMA; ETWNINI; -.
DR OrthoDB; 1709134at2; -.
DR BioCyc; MGEN243273:G1GJ2-106-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR CDD; cd00984; DnaB_C; 1.
DR Gene3D; 1.10.860.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF03796; DnaB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Primosome; Reference proteome.
FT CHAIN 1..468
FT /note="Replicative DNA helicase"
FT /id="PRO_0000102025"
FT DOMAIN 189..462
FT /note="SF4 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT BINDING 220..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT CONFLICT 267..270
FT /note="HESQ -> CMKS (in Ref. 2; AAD12329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 53884 MW; 88534526DD33561E CRC64;
MGQQTSFKYA NDSNIERAER RLMQAVAQNS EGIDLIFNKL EPIDFFATPF KLIFQTAKEN
YQLNNPIIGS GLLEAVKFKL DANDQSTKSE LEILFTKILL IRLPPNQTEI KTLVDVVKKA
SIFRRLQQFA KRVYNEEFKL KEDRFEGYLQ AIQDDFVKII HSAFSNIFAF SYDEIANQEE
ALIKKVHRGE LIISGLSSGF LKLDQLTSGW KPGELIVIAA RPGRGKTALL INFMASAAKQ
IDPKTDVVLF FSLEMRNREI YQRHLMHESQ TSYTLTNRQR INNVFEELME ASSRIKNLPI
KLFDYSSLTL QEIRNQITEV SKTSNVRLVI IDYLQLVNAL KNNYGLTRQQ EVTMISQSLK
AFAKEFNTPI IAAAQLSRRI EERKDSRPIL SDLRESGSIE QDADMVLFIH RTNDDKKEQE
EENTNLFEVE LILEKNRNGP NGKVKLNFRS DTSSFISQYS PSFDDQYS
