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Database: UniProt
Entry: C7NC96_LEPBD
LinkDB: C7NC96_LEPBD
Original site: C7NC96_LEPBD 
ID   C7NC96_LEPBD            Unreviewed;       451 AA.
AC   C7NC96;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   16-JAN-2019, entry version 73.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   OrderedLocusNames=Lebu_0001 {ECO:0000313|EMBL:ACV37938.1};
OS   Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 /
OS   NCTC 10249 / C-1013-b).
OC   Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=523794 {ECO:0000313|EMBL:ACV37938.1, ECO:0000313|Proteomes:UP000001910};
RN   [1] {ECO:0000313|EMBL:ACV37938.1, ECO:0000313|Proteomes:UP000001910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b
RC   {ECO:0000313|Proteomes:UP000001910};
RX   PubMed=21304648; DOI=10.4056/sigs.1854;
RA   Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA   Bruce D., Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S.,
RA   Mikhailova N., Pati A., Mavrommatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Rohde C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Leptotrichia buccalis type strain (C-
RT   1013-b).";
RL   Stand. Genomic Sci. 1:126-132(2009).
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, ECO:0000256|SAAS:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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; CP001685; ACV37938.1; -; Genomic_DNA.
DR   RefSeq; WP_012806132.1; NC_013192.1.
DR   ProteinModelPortal; C7NC96; -.
DR   STRING; 523794.Lebu_0001; -.
DR   EnsemblBacteria; ACV37938; ACV37938; Lebu_0001.
DR   KEGG; lba:Lebu_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; FPAFKIV; -.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; LBUC523794:G1GFL-1-MONOMER; -.
DR   Proteomes; UP000001910; 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   Gene3D; 3.30.300.180; -; 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   PANTHER; PTHR30050:SF2; PTHR30050:SF2; 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.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756129};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001910};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001910}.
FT   DOMAIN      140    279       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      356    427       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     148    155       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      307    334       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   451 AA;  51862 MW;  03B6685F62206854 CRC64;
     MNVGKLWEKI KKIMKKRVSE AEFEAFFKNV EATKLEDNKL TLVCNSKLIQ QNVGKYKGQM
     EEIAEIITDE IITIDFEIKK QDIMSYKPEI HSFSRESKEK SSAIYTGLNP KHRFDNFIVG
     ENSKLAYNAC LAVVNNPTPV YNPLFIYGSS GLGKTHLMQA VGNEILENNP NKRVYYSTSE
     EFANEFFKVL NGGRIQHFRD TFRALDVLLL DDIQFFEKVF GRGEGTVEEE FFHTFNKLQE
     LGKQIIMISD KSPKEIKNLS KRLESRFLSG LTVEIQSPGF ETRMMILKNM AKTQDIEIDD
     SILEYISDSL NTNVRELEGT LTNLNARAKL LNEKITLQLV QEMLMHNVKR EQSKITAKKV
     MEQISSQYGV SINDMISKKR QKKVVETRQI AMYLLKNNDD LDLSLTAIGG LFGGKDHSTV
     ISSIRKVEKK TREDVLFKKE IDMLNKKIFK V
//
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