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Database: UniProt
Entry: A0A0Q4G4X9_9SPHN
LinkDB: A0A0Q4G4X9_9SPHN
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ID   A0A0Q4G4X9_9SPHN        Unreviewed;       496 AA.
AC   A0A0Q4G4X9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=ASE75_03380 {ECO:0000313|EMBL:KQM67930.1};
OS   Sphingomonas sp. Leaf17.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1735683 {ECO:0000313|EMBL:KQM67930.1, ECO:0000313|Proteomes:UP000051777};
RN   [1] {ECO:0000313|EMBL:KQM67930.1, ECO:0000313|Proteomes:UP000051777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf17 {ECO:0000313|EMBL:KQM67930.1,
RC   ECO:0000313|Proteomes:UP000051777};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM67930.1, ECO:0000313|Proteomes:UP000051777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf17 {ECO:0000313|EMBL:KQM67930.1,
RC   ECO:0000313|Proteomes:UP000051777};
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:KQM67930.1}.
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DR   EMBL; LMKL01000001; KQM67930.1; -; Genomic_DNA.
DR   RefSeq; WP_055928668.1; NZ_LMKL01000001.1.
DR   AlphaFoldDB; A0A0Q4G4X9; -.
DR   STRING; 1735683.ASE75_03380; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000051777; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051777}.
FT   DOMAIN          189..496
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   496 AA;  53763 MW;  0865F98EC3AFB7B9 CRC64;
     MATLAFPAPA SPEPQQLPRN VEAEAAMLGA MMIDNRLADD LVDRLEPAHF FEPCHGRIFA
     AIKTLRGNDM LATPVTLRPM FEADEGMREL GGPAYLAGLT GSGAGLIGAR QFAQQIYDLA
     MLRALVSVGR TLVDRALDTS EEVNPRAQIE LAEEELFKVA AEGVSENAVK TFAQATTAAV
     KMAERALNSG GNLSGVTTGI NSINAKIGGM HHSDLMILAG RPGMGKTSLA TNIAFNAARR
     WMRDMNDGIA PADSVGAKVA FFSLEMSADQ LATRILAEQS GISSESLRMG KISRAEFGQL
     AAAAAELENL PLFIDDTGGL SIGALHTRVR RLQRRHNNQI GLVVVDYLQL LSGSGKTGDG
     NRVQEISEIS RGLKTLAKDL NVPVLALSQL SRAVEQREDK TPMLSDLRES GSIEQDADMV
     WFVYREDYYV ASKEPKRPID GDSAKIFEDH ASWAAEMERV YGLAELIVAK QRHGATGKVR
     MKFDPTITKF SDLEEY
//
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