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Database: UniProt
Entry: A0A2I8DIA1_9BURK
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ID   A0A2I8DIA1_9BURK        Unreviewed;       486 AA.
AC   A0A2I8DIA1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
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   Name=dnaB {ECO:0000313|EMBL:AUT46990.1};
GN   ORFNames=C2U31_13915 {ECO:0000313|EMBL:AUT46990.1};
OS   Achromobacter sp. AONIH1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1758194 {ECO:0000313|EMBL:AUT46990.1, ECO:0000313|Proteomes:UP000236176};
RN   [1] {ECO:0000313|Proteomes:UP000236176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RX   PubMed=29437920;
RG   NISC Comparative Sequencing Program;
RA   Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA   Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA   Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.;
RT   "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT   Bacterial Plasmids Conferring Carbapenem Resistance.";
RL   MBio 9:e02011-e02017(2018).
RN   [2] {ECO:0000313|Proteomes:UP000236176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RA   Segre J.A., Mullikin J.;
RL   Submitted (JAN-2018) 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; CP026124; AUT46990.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I8DIA1; -.
DR   KEGG; achr:C2U31_13915; -.
DR   Proteomes; UP000236176; Chromosome.
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:UP000236176}.
FT   DOMAIN          199..464
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          466..486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   486 AA;  52943 MW;  1853BE1060DA3BB5 CRC64;
     MADEAGNRVQ PSRRAVHEGA RTMTGNAANV PPHNLTAEHA ILGGLLLDNE ALDRLGDLEP
     AQFYHHGHRL IFEGARSLIL RSRPADVITV HDYLLTMGKA EAIGGMAYLN SLVESTPSLA
     NIGRYAEIVR ETALLRQLTV AADRVQQLVA ERHQPAVELL DAAQAEFSKL ALGAVQDEPV
     SISSAMVDFL DDLDGRVHGT VAHPGIATGI EALDEKLNGG PCRGDLVVIA GRPGMGKSAL
     AQSIGCNNAE AGYSVTFWSG EMPTKQVTGR SVANWGRVSS AKLNAAKPVL TPDEWTRLTR
     AAQIAGEARF FVEDAPALTI QALSAKARTV HRKHGLDVLI VDYLQLMEGS EQNRTLQIEA
     ITKGLKRLAK QLNIVVYALS QFSREIEKRV NKRPMLSDLR DGGSIEQDAD IAIGLYREEQ
     DDPDTTLKGY AELYIMKQRN GTLGMVPAAY RGEYLRFEDY TGPAVTKSSA KGKRGRRTFE
     DEEEAF
//
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