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Database: UniProt
Entry: A0A223NWW7_9SPHI
LinkDB: A0A223NWW7_9SPHI
Original site: A0A223NWW7_9SPHI 
ID   A0A223NWW7_9SPHI        Unreviewed;       462 AA.
AC   A0A223NWW7;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-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=MuYL_2480 {ECO:0000313|EMBL:ASU34367.1};
OS   Mucilaginibacter xinganensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1234841 {ECO:0000313|EMBL:ASU34367.1, ECO:0000313|Proteomes:UP000215002};
RN   [1] {ECO:0000313|EMBL:ASU34367.1, ECO:0000313|Proteomes:UP000215002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BJC16-A31 {ECO:0000313|EMBL:ASU34367.1,
RC   ECO:0000313|Proteomes:UP000215002};
RG   Henan University of Science and Technology;
RA   You X.;
RT   "Complete genome sequence of Mucilaginibacter sp. strain BJC16-A31.";
RL   Submitted (AUG-2017) 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; CP022743; ASU34367.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223NWW7; -.
DR   KEGG; muc:MuYL_2480; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000215002; 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:RHEA.
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; 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   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:ASU34367.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362085}; Primosome {ECO:0000256|RuleBase:RU362085};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215002}.
FT   DOMAIN          181..452
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   462 AA;  51794 MW;  EF5366901563415F CRC64;
     MSRNQTNYSG LGKLPPQSIE LEEAVLGAIM EMDVISTVID MLRPEMFYKT NHQIIYSVML
     SLAKQNEPID ELTVIATLRA SGELESVGGM FYVTELTRRV ASAANIEFNA RIIVQKFLAR
     EVIRISTEAI QTAYEDTTDV LELVEQVEKN IYDLSSHKNS KKQSKISDVV DECIEILSTP
     IKNGLTGIPT GLTNLDKLTN GWQDTDLIII AARPAMGKTA FVLHCAKYPA IKLNKPVLLF
     SLEMSEVQLG NRMIADEAGI CLDDIQKRNL SPYDKEKVIS LTRNLKKSPL IIDDTPALNI
     LEFRAKCRRA KQQHDIKLII IDYLQLMVGD AGNRNGNREQ EIGSISRMLK AVAKELKVPV
     IALSQLSRKV EERANKMPML SDIRESGSIE QDADMVIFLH RPEYYGITEF EGKSVVGKLS
     AIIAKHRNGV CDTAQLDLNA AYMRLTDWEI DFEPTELKGE SF
//
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