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Database: UniProt
Entry: V4YLH3_9PROT
LinkDB: V4YLH3_9PROT
Original site: V4YLH3_9PROT 
ID   V4YLH3_9PROT            Unreviewed;       482 AA.
AC   V4YLH3;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|ARBA:ARBA00018893, ECO:0000256|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:ESS15648.1};
GN   ORFNames=MOLA814_01230 {ECO:0000313|EMBL:ESS15648.1};
OS   Betaproteobacteria bacterium MOLA814.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1408164 {ECO:0000313|EMBL:ESS15648.1, ECO:0000313|Proteomes:UP000017838};
RN   [1] {ECO:0000313|EMBL:ESS15648.1, ECO:0000313|Proteomes:UP000017838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MOLA814 {ECO:0000313|EMBL:ESS15648.1,
RC   ECO:0000313|Proteomes:UP000017838};
RX   PubMed=24356832;
RA   Courties A., Riedel T., Jarek M., Intertaglia L., Lebaron P., Suzuki M.T.;
RT   "Genome Sequence of Strain MOLA814, a Proteorhodopsin-Containing
RT   Representative of the Betaproteobacteria Common in the Ocean.";
RL   Genome Announc. 1:e01062-13(2013).
CC   -!- FUNCTION: Plays an important role in the initiation and regulation of
CC       chromosomal replication. Binds to the origin of replication; it binds
CC       specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-
CC       TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
CC       {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00377}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|ARBA:ARBA00006583,
CC       ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU004227}.
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:ESS15648.1}.
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DR   EMBL; AYMW01000001; ESS15648.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4YLH3; -.
DR   STRING; 1408164.MOLA814_01230; -.
DR   PATRIC; fig|1408164.3.peg.213; -.
DR   eggNOG; COG0593; Bacteria.
DR   Proteomes; UP000017838; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.30.300.180; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00377; DnaA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001957; Chromosome_initiator_DnaA.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR018312; Chromosome_initiator_DnaA_CS.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR024633; DnaA_N_dom.
DR   InterPro; IPR038454; DnaA_N_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   NCBIfam; TIGR00362; DnaA; 1.
DR   PANTHER; PTHR30050; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR   PANTHER; PTHR30050:SF2; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 1.
DR   Pfam; PF11638; DnaA_N; 1.
DR   PRINTS; PR00051; DNAA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00760; Bac_DnaA_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48295; TrpR-like; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00377};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00377}; Reference proteome {ECO:0000313|Proteomes:UP000017838}.
FT   DOMAIN          179..313
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          390..459
FT                   /note="Chromosomal replication initiator DnaA C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00760"
FT   BINDING         187..194
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   482 AA;  54117 MW;  471AD2FD2F8FA3E1 CRC64;
     MWCTRSLYMS DDSFATISPA AWQHDLWPAC VDYLAQRIPD QQFNTWIRPL GAAVSTAPLQ
     VTLQVANRFK LDWIRSQYVQ KISAVLSQLA GQDVVVELAL TPRVATKTVS NLSQSFSQSR
     AGNDVLAEAL DVPTVRMPTD DAHKNRLNPA LTFDTLIEGS ANRMARAAAM HVASQLGQLY
     NPLFIYGGVG LGKTHLMHAI GNHLIGDQAN AKVLYIHAEQ FVSDVVKAYQ RKAFDEFKAR
     YHSLDLLLID DVQFFANKER TQEEFFNAFE ALLANRSHIV MTSDTYPKGL ADIHERLVSR
     FDSGLTVAIE PPELEMRVAI LINKAAVEGA HMPEDVAFFV AKNVRSNVRE LEGALRKILA
     YSRFNQKDIS IALAKEALRD LLSIQNRQIS VENIQKTVAD FYKIKIADMY SKKRPANIAR
     PRQIAMYLAK ELTQKSLPEI GEMFGGRDHT TVLHAVRKMA SERAQNTELN QQLHVLEQTL
     KG
//
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