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Database: UniProt
Entry: S7VKE8_9FLAO
LinkDB: S7VKE8_9FLAO
Original site: S7VKE8_9FLAO 
ID   S7VKE8_9FLAO            Unreviewed;       475 AA.
AC   S7VKE8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=ADIWIN_3511 {ECO:0000313|EMBL:EPR70650.1};
OS   Winogradskyella psychrotolerans RS-3.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=641526 {ECO:0000313|EMBL:EPR70650.1, ECO:0000313|Proteomes:UP000014962};
RN   [1] {ECO:0000313|EMBL:EPR70650.1, ECO:0000313|Proteomes:UP000014962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS-3 {ECO:0000313|EMBL:EPR70650.1,
RC   ECO:0000313|Proteomes:UP000014962};
RX   PubMed=23950132;
RA   Kumar Pinnaka A., Ara S., Singh A., Shivaji S.;
RT   "Draft Genome Sequence of Winogradskyella psychrotolerans RS-3T, Isolated
RT   from the Marine Transect of Kongsfjorden, Ny-Alesund, Svalbard, Arctic
RT   Ocean.";
RL   Genome Announc. 1:e00630-e00613(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:EPR70650.1}.
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DR   EMBL; ATMR01000180; EPR70650.1; -; Genomic_DNA.
DR   RefSeq; WP_020896025.1; NZ_ATMR01000180.1.
DR   AlphaFoldDB; S7VKE8; -.
DR   STRING; 641526.ADIWIN_3511; -.
DR   PATRIC; fig|641526.4.peg.3478; -.
DR   eggNOG; COG0593; Bacteria.
DR   OrthoDB; 9807019at2; -.
DR   Proteomes; UP000014962; 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:UP000014962}.
FT   DOMAIN          172..308
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          383..452
FT                   /note="Chromosomal replication initiator DnaA C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00760"
FT   BINDING         180..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   475 AA;  54112 MW;  805D8FA491D323CC CRC64;
     MEITAQSVWS NCLAFIKDNI QPQAYKTWFE PIDAVKLSGN ALSIQVPSKF FYEWLEEHYV
     KILKVSLTKE LGEDAKLVYV IKMENTYGNK QPFTEKIPSA NRSALKSQDV DVPFNNKSPE
     LRNPFIIPGI RNVKIESQLN PSYSFENFLE GDSNRLARNA GIAVANKPGG TSFNPLLIFG
     GVGLGKTHLA HAIGVDIKDK YPEKTVLYIS AEKFTQQYID SVKKNNRNDF IHFYQIIDVL
     IIDDVQFLSG KTGTQDVFFH IFNHLHQNGK QVILTSDKAP VDMQDIEQRL LSRFKWGLSA
     ELQTPDFETR VSILKNKLYR DGVEMPEDII EYVAKHIKTN VRELEGAIIS LIAQSSFNKK
     EITISLAKDI VEKFVKNTKR EVSIDYIQKV VSDYFQMDVN TLQSKTRKRH IVQARQLAMF
     FAKKYTKASL ASIGSQIGQR DHATVLHACK TVDNLSSTDK QFRKYVEDLS KKLAL
//
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