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Database: UniProt
Entry: Q72G59_DESVH
LinkDB: Q72G59_DESVH
Original site: Q72G59_DESVH 
ID   Q72G59_DESVH            Unreviewed;       437 AA.
AC   Q72G59;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA-1 {ECO:0000313|EMBL:AAS94485.1};
GN   OrderedLocusNames=DVU_0001 {ECO:0000313|EMBL:AAS94485.1};
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Nitratidesulfovibrio.
OX   NCBI_TaxID=882 {ECO:0000313|EMBL:AAS94485.1, ECO:0000313|Proteomes:UP000002194};
RN   [1] {ECO:0000313|EMBL:AAS94485.1, ECO:0000313|Proteomes:UP000002194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC   {ECO:0000313|Proteomes:UP000002194};
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M., Daugherty S.C.,
RA   Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C.,
RA   Sullivan S.A., Fouts D., Haft D.H., Selengut J., Peterson J.D.,
RA   Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M.,
RA   Tran K., Khouri H., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D.,
RA   Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
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|RuleBase:RU000577}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|ARBA:ARBA00006583,
CC       ECO:0000256|RuleBase:RU004227}.
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DR   EMBL; AE017285; AAS94485.1; -; Genomic_DNA.
DR   RefSeq; WP_010937312.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_009226.1; NC_002937.3.
DR   AlphaFoldDB; Q72G59; -.
DR   SMR; Q72G59; -.
DR   STRING; 882.DVU_0001; -.
DR   PaxDb; 882-DVU_0001; -.
DR   EnsemblBacteria; AAS94485; AAS94485; DVU_0001.
DR   KEGG; dvu:DVU_0001; -.
DR   PATRIC; fig|882.5.peg.1; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_3_2_7; -.
DR   OrthoDB; 9807019at2; -.
DR   PhylomeDB; Q72G59; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   Gene3D; 3.30.300.180; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR038454; DnaA_N_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
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   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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000577};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU000577};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000577};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000577};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002194}.
FT   DOMAIN          136..264
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          342..411
FT                   /note="Chromosomal replication initiator DnaA C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00760"
SQ   SEQUENCE   437 AA;  49501 MW;  285436BB6A83E002 CRC64;
     MLQQALRQHL RQTCSEQELH QWFDPLDLRL DDAQQRLEVR FPHPHFARWF EAQALERFTA
     GVRDVVGTSV ALVFPEGIKT TDRSTVQPPS QPPLASESVA CPFGAAFTFD AFITNRKNQF
     PLAAAREAAR NGHQRTYNPF VLCGASGNGK THLLRALANE LAALYGTDAV FCGSAEELHD
     RYNTEERLAM RRTLCAHRAL LLDDLHRLRA LPDLREELTA LFDHFYDHGK QMAFAYAGRL
     SDLDFLEAPL RSRLELGLIV DLKEPDLDVR VRYIHARCAA LSLQLAREHV LTLAQRCHEF
     RHLSGLLLKV AAYRDMVGRD ILDRELEQIL RNTDSGPERA VAPDTIISAA AEHFGVTPRD
     ILSDKRQQHI VQARQVAMFL CRELIGSSFP ALGRMFGGKD HSTAMYAVKK IKKLQYDNKD
     MHALVAELKR RCLNHDG
//
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