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Database: UniProt
Entry: B0VID0_CLOAI
LinkDB: B0VID0_CLOAI
Original site: B0VID0_CLOAI 
ID   B0VID0_CLOAI            Unreviewed;       443 AA.
AC   B0VID0;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-SEP-2017, entry version 72.
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:CAO79919.1};
GN   OrderedLocusNames=CLOAM0001 {ECO:0000313|EMBL:CAO79919.1};
OS   Cloacimonas acidaminovorans (strain Evry).
OC   Bacteria; Candidatus Cloacimonetes; Candidatus Cloacimonas.
OX   NCBI_TaxID=459349 {ECO:0000313|EMBL:CAO79919.1, ECO:0000313|Proteomes:UP000002019};
RN   [1] {ECO:0000313|EMBL:CAO79919.1, ECO:0000313|Proteomes:UP000002019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Evry {ECO:0000313|Proteomes:UP000002019};
RX   PubMed=18245282; DOI=10.1128/JB.01248-07;
RA   Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R.,
RA   Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C.,
RA   Weissenbach J., Le Paslier D.;
RT   "'Candidatus Cloacamonas acidaminovorans': genome sequence
RT   reconstruction provides a first glimpse of a new bacterial division.";
RL   J. Bacteriol. 190:2572-2579(2008).
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|RuleBase:RU000577}.
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; CU466930; CAO79919.1; -; Genomic_DNA.
DR   RefSeq; WP_015423780.1; NC_020449.1.
DR   ProteinModelPortal; B0VID0; -.
DR   KEGG; caci:CLOAM0001; -.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   Proteomes; UP000002019; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR024633; DnaA_N_dom.
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   Pfam; PF11638; DnaA_N; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002019};
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|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002019}.
FT   DOMAIN      136    270       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      350    420       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     144    151       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   443 AA;  51502 MW;  A0201FB903AC3272 CRC64;
     MDQDIWQNIL DKLEENINPQ SFKTWFSDTR LVDMNDRELM IRVATQFSAN YLNQNYKEVL
     GEISYGLYGR KYDVQFITQP HRNHNKEKDV QDYSIKRVSA NVRLNERYTF DEFVVGKNNN
     FAYSAAKAVA ESPGYTYNPL FIYGESGMGK THLMQAIGNY ILKEGRNCSI YYITSEAFTN
     EMIDGIRSNK MPEFRAKFRK VDLLLMDDIH FLSRKEGTQE EFFHTFNALF ENKKQIVLTS
     DRPPKDIPDL EKRLVTRFES GLLCDLKSPD FETRVAILRK KAEPENVVLS DAIFNFIADN
     ITSSVRALEG SLIRILAFSS YNKLNPEDID INLAAEILSD MISEKVHSIT LDAITEKVCE
     CYGITPAQLL EKTRKPQVAF PRQVAMYLAN YLIPQLSLKD IAEYYNRKDH TTVLHAKKMV
     ENQFREKEDF RIQLEEIIKN LKK
//
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