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Database: UniProt
Entry: A0A0T0PTS1_9SPHN
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ID   A0A0T0PTS1_9SPHN        Unreviewed;       496 AA.
AC   A0A0T0PTS1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=ASG29_10710 {ECO:0000313|EMBL:KQT32280.1};
OS   Sphingomonas sp. Leaf412.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT32280.1, ECO:0000313|Proteomes:UP000051178};
RN   [1] {ECO:0000313|EMBL:KQT32280.1, ECO:0000313|Proteomes:UP000051178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32280.1,
RC   ECO:0000313|Proteomes:UP000051178};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT32280.1, ECO:0000313|Proteomes:UP000051178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32280.1,
RC   ECO:0000313|Proteomes:UP000051178};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQT32280.1}.
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DR   EMBL; LMQP01000003; KQT32280.1; -; Genomic_DNA.
DR   RefSeq; WP_055983577.1; NZ_LMQP01000003.1.
DR   AlphaFoldDB; A0A0T0PTS1; -.
DR   STRING; 1736370.ASG29_10710; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000051178; 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:RHEA.
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; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051178}.
FT   DOMAIN          189..496
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   496 AA;  54277 MW;  EE66C4A9B1EB1F6F CRC64;
     MATLAFPHPA PAEPIQLPRN VEAEAAMLGA MLIDNRLADD IVDRLEPQHF YEPVHGRVFA
     AIKTLRGKDM LASPVTLRPM FEADEGMREL GGPAYLAQLT GSGAGLIGAR QFANQIYDLA
     MLRSLVTVGR TLVDRAMDTS EEVNPRAQIE LAEEELFKVS ADGQSESTVK SFAQAATMAV
     RMAEKALNWG GNLSGVTTGL DSINAKIGGL HHSDLMILAG RPGMGKTSLA TNIAFNAAQR
     WMHDMRDGIP PAKSVGAKVA FFSLEMSADQ LATRILAEQS RISSEALRMG KISKSEFEQL
     AAAAVELENL PLFIDDTGGL SIGALHTRVR RLQRRHNNEI GLVVVDYLQL LSGSGKTGDG
     NRVQEISEIS RGLKTLAKDM NVPVLALSQL SRAVEQREDK RPQLSDLRES GSIEQDADMV
     WFVFREDYYI AAKEPKRPAE GDDTRAFEDH ARWAADMERV YGLAELIVAK QRHGATGKVT
     LKFDPTITRF SDYAGY
//
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