ID D6ZJW0_MOBCV Unreviewed; 483 AA.
AC D6ZJW0;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 76.
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 ECO:0000313|EMBL:ADI67009.1};
GN OrderedLocusNames=HMPREF0573_10690 {ECO:0000313|EMBL:ADI67009.1};
OS Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125) (Falcivibrio
OS vaginalis).
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Mobiluncus.
OX NCBI_TaxID=548479 {ECO:0000313|EMBL:ADI67009.1, ECO:0000313|Proteomes:UP000006742};
RN [1] {ECO:0000313|Proteomes:UP000006742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43063 / DSM 2711 / V125
RC {ECO:0000313|Proteomes:UP000006742};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP001992; ADI67009.1; -; Genomic_DNA.
DR RefSeq; WP_004007803.1; NC_014246.1.
DR AlphaFoldDB; D6ZJW0; -.
DR STRING; 548479.HMPREF0573_10690; -.
DR GeneID; 55564843; -.
DR KEGG; mcu:HMPREF0573_10690; -.
DR eggNOG; COG0593; Bacteria.
DR HOGENOM; CLU_026910_2_0_11; -.
DR Proteomes; UP000006742; Chromosome.
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; 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 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 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|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:UP000006742}.
FT DOMAIN 174..302
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 386..455
FT /note="Chromosomal replication initiator DnaA C-terminal"
FT /evidence="ECO:0000259|SMART:SM00760"
FT BINDING 182..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ SEQUENCE 483 AA; 53015 MW; AF899F864053AA13 CRC64;
MDNAAWESAA KADLGPTDFW AKALENLSVS GKIGNFDLAL IRQSKGLGES GDAAVLAVSS
NDVKTMIESK YSDLFKTTFS EVLHRPINNL IVTVDENLGN MAPTPQTFEP VAPQPAPPIA
PTTPVWEPEH QQTLHIDSNT GLNPTYTFDS FVIGSSNSFT AAAAESVVAS PAKAYNPLFI
YGGPGLGKTH LLHAIGNYAL ELYPDSKVKY ISSEEFTNEF INAIASQTFA EFQARYREVD
FLLIDDIQFL AGKEQTLEEF FHTFNTLHTA QKQVVITSDV APKELKGFEE RVRSRLEWGL
MADIQPPSLE TRIAILRRKA QAGNMQMPDD VAEFIASNVD SDIRALEGAL IRVTAYWSLN
HVPATIETAK LAIRDLMTGK GAKEITPEMI IDCTAQYFSL TSEDLLSANR SRTVVGPRQI
AMYLCRELTD LSLPQVGAAF GGRDHTTVMH ANKKVAASMK EDTQTFKSVS DISDAVRRAT
RES
//
