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Database: UniProt
Entry: C2KY12_9FIRM
LinkDB: C2KY12_9FIRM
Original site: C2KY12_9FIRM 
ID   C2KY12_9FIRM            Unreviewed;       381 AA.
AC   C2KY12;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   25-OCT-2017, entry version 58.
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:EEJ51341.1};
GN   ORFNames=HMPREF6123_1401 {ECO:0000313|EMBL:EEJ51341.1};
OS   Oribacterium sinus F0268.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Oribacterium.
OX   NCBI_TaxID=585501 {ECO:0000313|EMBL:EEJ51341.1, ECO:0000313|Proteomes:UP000004121};
RN   [1] {ECO:0000313|EMBL:EEJ51341.1, ECO:0000313|Proteomes:UP000004121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0268 {ECO:0000313|EMBL:EEJ51341.1,
RC   ECO:0000313|Proteomes:UP000004121};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C.,
RA   Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L.,
RA   Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y.,
RA   Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L.,
RA   Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F.,
RA   Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M.,
RA   Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S.,
RA   Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J.,
RA   Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J.,
RA   Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D.,
RA   Worley K., Gibbs R.;
RL   Submitted (APR-2009) 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:SAAS00747914}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EEJ51341.1}.
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DR   EMBL; ACKX01000128; EEJ51341.1; -; Genomic_DNA.
DR   ProteinModelPortal; C2KY12; -.
DR   STRING; 585501.HMPREF6123_1401; -.
DR   EnsemblBacteria; EEJ51341; EEJ51341; HMPREF6123_1401.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000004121; Unassembled WGS sequence.
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; 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   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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004121};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004121}.
FT   DOMAIN       74    211       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      289    358       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND      82     89       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   381 AA;  43255 MW;  90F6ABFE5860AED5 CRC64;
     MEITGIYTEI LITDEEGLKE LYPKKNQEEQ PGLEEALKNA NLNSRYTFDS FVVGSSNALA
     HAACVAAAEM PGEQYNPLYI YGGAGLGKTH LMQSVAHYIL QQNKNAKIRY VTSETFINEF
     VDSIRNKNNI SPAEFRRKYR ELDVLLIDDI QFLIGKEGTQ EEFFHTFNAL YDNRKQIIIA
     SDKPPKKIDN IEERLLSRFE VGLTVDIQLP DVETRMAILR KKEELEGYNI DNEVIKYIAD
     NIKSNVRELE GALTKVVAKS RLIKQPVTLS LAEELLKDNI TPAEKKELTP KWIIEVVAEH
     HGLSLSDLVS KRKNKEIVIP RQIAMYLCRE MTSIPLNTVG ELLGGRDHST IIHGCDKISK
     ELSTNEQLQS TIEVLRKKIS P
//
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