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Database: UniProt
Entry: A0A0D6PCQ3_9PROT
LinkDB: A0A0D6PCQ3_9PROT
Original site: A0A0D6PCQ3_9PROT 
ID   A0A0D6PCQ3_9PROT        Unreviewed;       494 AA.
AC   A0A0D6PCQ3;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=Aam_017_016 {ECO:0000313|EMBL:GAN79111.1};
OS   Acidocella aminolytica 101 = DSM 11237.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidocella.
OX   NCBI_TaxID=1120923 {ECO:0000313|EMBL:GAN79111.1, ECO:0000313|Proteomes:UP000032668};
RN   [1] {ECO:0000313|EMBL:GAN79111.1, ECO:0000313|Proteomes:UP000032668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=101 / DSM 11237 {ECO:0000313|Proteomes:UP000032668};
RA   Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT   "Whole genome sequence of Acidocella aminolytica 101 = DSM 11237.";
RL   Submitted (NOV-2012) 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:GAN79111.1}.
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DR   EMBL; BANC01000017; GAN79111.1; -; Genomic_DNA.
DR   RefSeq; WP_048877579.1; NZ_FQVJ01000006.1.
DR   AlphaFoldDB; A0A0D6PCQ3; -.
DR   STRING; 1120923.SAMN02746095_00944; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000032668; 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:UP000032668}.
FT   DOMAIN          188..493
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   494 AA;  54569 MW;  DB1E88D8CFF84717 CRC64;
     MDSIDQTPSG LPRRLPPSNT QAEQALLGAL LANNKAFERV SDFLAPEHFA DPIHGRIYQA
     IARRCEQNQV ADPITLRAEL EHAGVLEEVG GTAYLAQLLS AMVGIINAGD YGRLIHDAWL
     RRQLIDIGEL MVNDAYASEA ELDGRAQIEK SEQSLFNLAT KGGSEGKGVS FHDALVAAIE
     LAEKAFRNQG SVSGLDTGLR DLNKRTGGLH KSDLIILAGR PGMGKTALVT KVAFGAAKAM
     LNNARAENPN AMAKECVVIF SLEMSADQLA TRLLAEQAMV SGDKIRRGEI STKDFDTFVR
     VSREIADVPL VIDDTPAITL SALRTRCRRL QRTQGLGLVI VDYLQLMRPA LGTKPESRVL
     EISQITQGLK AIAKELAVPV IALSQLSRSV ESRDDKRPQL SDLRESGSIE QDADMVMFIY
     RDEYYLAQRE PKITNFDRDD KFQEAHEKWQ ADMQSVYQKA ELIIAKQRHG PTGKIDLFFE
     GEFTRFADLD TLHE
//
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