ID A0A1D7XR18_9FLAO Unreviewed; 512 AA.
AC A0A1D7XR18;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-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=FORMA_05830 {ECO:0000313|EMBL:AOR25758.1};
OS Formosa sp. Hel3_A1_48.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1336795 {ECO:0000313|EMBL:AOR25758.1, ECO:0000313|Proteomes:UP000094318};
RN [1] {ECO:0000313|EMBL:AOR25758.1, ECO:0000313|Proteomes:UP000094318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel3_A1_48 {ECO:0000313|EMBL:AOR25758.1,
RC ECO:0000313|Proteomes:UP000094318};
RA Unfried F., Harder J., Teeling H., Hahnke R.L., Markert S., Kappelmann L.,
RA Chafee M.;
RT "Glycan utilization in Formosa spp.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in initiation and elongation during chromosome
CC replication; it exhibits DNA-dependent ATPase activity.
CC {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; CP017259; AOR25758.1; -; Genomic_DNA.
DR RefSeq; WP_069674224.1; NZ_CP017259.1.
DR AlphaFoldDB; A0A1D7XR18; -.
DR STRING; 1336795.FORMA_05830; -.
DR KEGG; foh:FORMA_05830; -.
DR PATRIC; fig|1336795.4.peg.553; -.
DR OrthoDB; 9773982at2; -.
DR Proteomes; UP000094318; 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|RuleBase:RU362085, ECO:0000313|EMBL:AOR25758.1};
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:UP000094318}.
FT DOMAIN 194..469
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 487..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 57363 MW; B2BB0041A6EE2A95 CRC64;
MKQPESYKNF ATDRSKIISL EQGKIPPQAI DLEEVVLGAM MIDKKGVDEV IDILSIESFY
KQAHQHIFEA ILLLFESSQP IDLLTVSSQL RKNQKLDIVG GDFYLIGLTQ KVSSSAHIEF
HARIILQKFI QRSLIKISNE IIEDSFDETK DVFDLLDKAE SKLYDVTQGN IKKSTETAQD
LVFQAKRKIE EISNKEGLSG IPSGFDKVDK LTSGWQESDL IIVAARPGMG KTALTLSMAR
NIAVNQNIPV AFFSLEMSSV QLITRLISSE TGLSSEKLRT GKLEKHEWEQ LNVKVKSLEK
APLYIDDTPS LSIFDLRAKA RRLASQNGIK LIIVDYLQLM TAGGSQKTGN REQEISMISR
NLKALAKELS VPVIALSQLS RAVETRGGSK RPLLSDLRES GAIEQDADIV SFIYRPEYYK
IEEWDDEEHT PCEGQAEFII AKHRNGGLDN IRLKFIGHLG KFDNLDNFDS PFDAEFHSKM
NAAANDDTFA EDNSIQMDPN DAFGPPDDDT PY
//
