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Database: UniProt
Entry: I4ZCE2_9BACT
LinkDB: I4ZCE2_9BACT
Original site: I4ZCE2_9BACT 
ID   I4ZCE2_9BACT            Unreviewed;       467 AA.
AC   I4ZCE2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   05-JUL-2017, entry version 35.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=PrebiDRAFT_2237 {ECO:0000313|EMBL:EIM33884.1};
OS   Prevotella bivia DSM 20514.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=868129 {ECO:0000313|EMBL:EIM33884.1, ECO:0000313|Proteomes:UP000002786};
RN   [1] {ECO:0000313|EMBL:EIM33884.1, ECO:0000313|Proteomes:UP000002786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20514 {ECO:0000313|EMBL:EIM33884.1,
RC   ECO:0000313|Proteomes:UP000002786};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Munk A.C.C., Kyrpides N., Mavromatis K.,
RA   Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "Improved High-Quality Draft genome of Prevotella bivia DSM 20514.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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:SAAS00724167}.
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; JH660658; EIM33884.1; -; Genomic_DNA.
DR   RefSeq; WP_004336234.1; NZ_JH660658.1.
DR   EnsemblBacteria; EIM33884; EIM33884; PrebiDRAFT_2237.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002786; Unassembled WGS sequence.
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; 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.
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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002786};
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:UP000002786}.
FT   DOMAIN      163    291       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      374    443       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     171    178       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   467 AA;  53166 MW;  EA826F35291E2A3C CRC64;
     MSVSPNSLWE QCLCLIAENV TEQQYNTWFK PLVFKSYQPA TKRLLVLVPS MFVYEYLEEH
     YVDLLKKVLT RVFGERVMLT YSVITDKDHQ LTQDLQAEDI DPIDSKRPTV RGNQSPTVID
     AVLPDIDSQL DPHKSFNNYV EGDSNKMPLT IGLAIAEHPN KNQFNPLFIY GPSGCGKTHL
     INAIGLKVKK LYPQKRVLYV SARLFQVQYT NSVRTNTTND FINFYQTIDV LIVDDIQEWM
     TATKTQDTFF HIFNHLFRNG KRIILASDRP PVDLEGMNDR LLTRFVAGLI TELEKPNIQL
     CVDILHSKIK RDGLIIPENV IQFIAQTANG SVRDLQGVIN SLLAYSVVYN SSIDMRLAER
     VIKRAVKIDD EPLTIDDILD KVCNHFNVTQ AAVNSRSRKK DIVIARQVAM YMAQKYTKMP
     ASRIGKLVGG RDHSTVIHSC AKIEDRLQVD KGFTAELAAI ENSFKLK
//
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