ID Q899S5_CLOTE Unreviewed; 342 AA.
AC Q899S5;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 07-JUN-2017, entry version 121.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN ECO:0000313|EMBL:AAO34747.1};
GN OrderedLocusNames=CTC_00094 {ECO:0000313|EMBL:AAO34747.1};
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO34747.1, ECO:0000313|Proteomes:UP000001412};
RN [1] {ECO:0000313|EMBL:AAO34747.1, ECO:0000313|Proteomes:UP000001412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of
RT tetanus disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC -!- FUNCTION: Plays an important role in the initiation and regulation
CC of chromosomal replication. Binds to the origin of replication; it
CC binds specifically double-stranded DNA at a 9 bp consensus (dnaA
CC box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic
CC phospholipids. {ECO:0000256|HAMAP-Rule:MF_00377,
CC ECO:0000256|SAAS:SAAS00731907}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC ECO:0000256|SAAS:SAAS00756131}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC ECO:0000256|SAAS:SAAS00555179}.
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DR EMBL; AE015927; AAO34747.1; -; Genomic_DNA.
DR ProteinModelPortal; Q899S5; -.
DR STRING; 212717.CTC00094; -.
DR EnsemblBacteria; AAO34747; AAO34747; CTC_00094.
DR KEGG; ctc:CTC_00094; -.
DR eggNOG; ENOG4105CI4; Bacteria.
DR eggNOG; COG0593; LUCA.
DR OMA; REFNPLF; -.
DR OrthoDB; POG091H02FF; -.
DR Proteomes; UP000001412; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
DR CDD; cd06571; Bac_DnaA_C; 1.
DR Gene3D; 1.10.1750.10; -; 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; IPR027417; P-loop_NTPase.
DR InterPro; IPR010921; Trp_repressor/repl_initiator.
DR PANTHER; PTHR30050:SF12; PTHR30050:SF12; 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; SSF48295; SSF48295; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00362; DnaA; 1.
DR PROSITE; PS01008; DNAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|SAAS:SAAS00731922};
KW Complete proteome {ECO:0000313|Proteomes:UP000001412};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|SAAS:SAAS00756112};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|SAAS:SAAS00756124};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW ECO:0000256|SAAS:SAAS00731897};
KW Reference proteome {ECO:0000313|Proteomes:UP000001412}.
FT DOMAIN 37 165 AAA. {ECO:0000259|SMART:SM00382}.
FT DOMAIN 249 318 Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT NP_BIND 45 52 ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ SEQUENCE 342 AA; 38871 MW; 9ECC1D6A1F87330E CRC64;
MSAMLNPKYT FDSFVIGNSN RFAHAASLAV AEAPAKAYNP LFIYGGVGLG KTHLMHAIGH
YILQNNSNVK VVYVSSEKFT NELINSIKDD KNEEFRNKYR NVDVLLIDDI QFIAGKERTQ
EEFFHTFNAL HEANKQIILS SDRPPKEIPT LEDRLRSRFE WGLIADIQAP DFETRMAILK
KKADVEHLNI PNEVMVYIAT KIKSNIRELE GALIRIVAFS SLTNKEISVD LASEALKDII
SSKESNQVTI ELIQDIVSSY FNLRVEDFKS SRRTRNVAFP RQIAMYLCRK LTDNSLPKIG
EEFGGRDHTT VIHGYEKIST ALKKDDSLQK TVNELTSKIN QK
//
