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Database: UniProt
Entry: A0A1J5IBX9_9GAMM
LinkDB: A0A1J5IBX9_9GAMM
Original site: A0A1J5IBX9_9GAMM 
ID   A0A1J5IBX9_9GAMM        Unreviewed;       473 AA.
AC   A0A1J5IBX9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Replicative DNA helicase {ECO:0000256|ARBA:ARBA00021957, ECO:0000256|RuleBase:RU362085};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU362085};
GN   ORFNames=AUK56_07835 {ECO:0000313|EMBL:OIP94708.1};
OS   Thiomicrospira sp. CG2_30_44_34.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=1805397 {ECO:0000313|EMBL:OIP94708.1, ECO:0000313|Proteomes:UP000182935};
RN   [1] {ECO:0000313|EMBL:OIP94708.1, ECO:0000313|Proteomes:UP000182935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG2_30_44_34 {ECO:0000313|EMBL:OIP94708.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
CC   -!- FUNCTION: Participates in initiation and elongation during chromosome
CC       replication; it exhibits DNA-dependent ATPase activity and contains
CC       distinct active sites for ATP binding, DNA binding, and interaction
CC       with DnaC protein, primase, and other prepriming proteins.
CC       {ECO:0000256|ARBA:ARBA00003574, ECO:0000256|RuleBase:RU362085}.
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         Evidence={ECO:0000256|ARBA:ARBA00001665,
CC         ECO:0000256|RuleBase:RU362085};
CC   -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008428, ECO:0000256|RuleBase:RU362085}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OIP94708.1}.
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DR   EMBL; MNZS01000054; OIP94708.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J5IBX9; -.
DR   STRING; 1805397.AUK56_07835; -.
DR   Proteomes; UP000182935; Unassembled WGS sequence.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR   CDD; cd00984; DnaB_C; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR   InterPro; IPR007692; DNA_helicase_DnaB.
DR   InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR   InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00665; DnaB; 1.
DR   PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1.
DR   PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1.
DR   Pfam; PF00772; DnaB; 1.
DR   Pfam; PF03796; DnaB_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51199; SF4_HELICASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362085};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU362085};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362085};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU362085};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362085};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|RuleBase:RU362085}.
FT   DOMAIN          182..467
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   473 AA;  52495 MW;  2E0967A8EBBB2A5D CRC64;
     MSQEALFKTP PHSIESEQSV IGGLLLDNEK LSDVSVILRE FDFYTQAHQL IYGAILTLNE
     RNKPFDVVTI IEYLESIGKL ADAGDKAYLV DLVSNTPGSV NIEFYADIVR QKAILRALIT
     VSNEISEASY FPQGREISEV LDLAESKVMQ IAEHGSGQQR DYQTMRDLLN QALTTIDERF
     NSDGTITGMA TKFSDFDEVT SGLQKGDLVI VAGRPSMGKT TFSMNMAENI ALQGVPVAVF
     SMEMPGSQLV LRMISSLGRI EADRIRTGKL QDEDWHNLNR AVSQLTSANV YIDDSPALMI
     TDLRARARRI DKDVREEQYK AAEAAGAEDP AAQVTGLGLI VIDYLQLMRG STNTDNRVNE
     ISEISRGLKS IAKELNVPVV ALSQLSRNLE QRPDKRPKMA DLRESGAIEQ DADLIIFIYR
     DEVYHPDSDD KGTAEIILGK HRNGALANVR LTFIGQYTKF ENHAGFNVPD DPY
//
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