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Database: UniProt
Entry: A0A248JVS1_9PROT
LinkDB: A0A248JVS1_9PROT
Original site: A0A248JVS1_9PROT 
ID   A0A248JVS1_9PROT        Unreviewed;       502 AA.
AC   A0A248JVS1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=Y958_17000 {ECO:0000313|EMBL:ASG22620.1};
OS   Nitrospirillum amazonense CBAmc.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Nitrospirillum.
OX   NCBI_TaxID=1441467 {ECO:0000313|EMBL:ASG22620.1, ECO:0000313|Proteomes:UP000197153};
RN   [1] {ECO:0000313|EMBL:ASG22620.1, ECO:0000313|Proteomes:UP000197153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBAmC {ECO:0000313|EMBL:ASG22620.1,
RC   ECO:0000313|Proteomes:UP000197153};
RA   Schwab S., dos Santos Teixeira K.R., Simoes Araujo J.L., Soares Vidal M.,
RA   Borges de Freitas H.R., Rivello Crivelaro A.L., Bueno de Camargo Nunes A.,
RA   dos Santos C.M., Palmeira da Silva Rosa D., da Silva Padilha D.,
RA   da Silva E., Araujo Terra L., Soares Mendes V., Farinelli L.,
RA   Magalhaes Cruz L., Baldani J.I.;
RT   "Complete genome sequence of Nitrospirillum amazonense strain CBAmC, an
RT   endophytic nitrogen-fixing and plant growth-promoting bacterium, isolated
RT   from sugarcane.";
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; CP022111; ASG22620.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A248JVS1; -.
DR   KEGG; nao:Y958_17000; -.
DR   Proteomes; UP000197153; Chromosome 2.
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:UP000197153}.
FT   DOMAIN          194..493
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  55576 MW;  68664B9E19E4846C CRC64;
     MPMDTKLTDP TAPTGALPYR TPPHNLEAEQ ALLGAALVNN KALEKVAEFL RPEHFFDPAN
     GRVFAAIAKL VERGQIASPL TLKAYFEQDA DLKEIGGTEY LARLAAGVVT VSNAEDYGRI
     IHDAYLRRQL IDVGEDMVNA AYKHDLDVVA TDQIEEAEKK LFDLASTGDA QGGFIPFERS
     LKAAIEMAEA AYKRSSHVTG VTTGLRDLDG KLGGLHPSDL IILAGRPSMG KTALATNIAF
     NAARAHMKSS GKEGAPVGFF SLEMSAEQLA TRILADEAEV SGDKIRRGEI HGSDFPRFIE
     ASNYISKVPF FVDDTPALSI TAVRTRARRL KRTHGLGMIV VDYLQLLRGG GINKTDNRVQ
     EISEITRGLK AIAKELDLPV IALSQLSRQV ENREDKRPQL SDLRESGSIE QDADVVMFVY
     REQYYLERAE PSRRPEEAED KFNDRYQRWQ QRLEEVHDTA EAIIAKQRHG PVGTVRLHFH
     GEFTRFSDLD THHALAGAGD DY
//
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