GenomeNet

Database: UniProt
Entry: C2CYB8_LACBR
LinkDB: C2CYB8_LACBR
Original site: C2CYB8_LACBR 
ID   C2CYB8_LACBR            Unreviewed;       469 AA.
AC   C2CYB8;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   25-OCT-2017, entry version 57.
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   ECO:0000313|EMBL:EEI72423.1};
GN   ORFNames=HMPREF0496_0290 {ECO:0000313|EMBL:EEI72423.1};
OS   Lactobacillus brevis subsp. gravesensis ATCC 27305.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=525310 {ECO:0000313|EMBL:EEI72423.1, ECO:0000313|Proteomes:UP000003176};
RN   [1] {ECO:0000313|EMBL:EEI72423.1, ECO:0000313|Proteomes:UP000003176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27305 {ECO:0000313|EMBL:EEI72423.1,
RC   ECO:0000313|Proteomes:UP000003176};
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 (JAN-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:SAAS00724167}.
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:EEI72423.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; ACGG01000010; EEI72423.1; -; Genomic_DNA.
DR   RefSeq; WP_003550988.1; NZ_GG669604.1.
DR   ProteinModelPortal; C2CYB8; -.
DR   EnsemblBacteria; EEI72423; EEI72423; HMPREF0496_0290.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000003176; 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; 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: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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003176};
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:UP000003176}.
FT   DOMAIN      166    297       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      378    447       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     174    181       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   469 AA;  53481 MW;  C3E0BC773725BC5F CRC64;
     MLELICISYN DYLIRGDFKV LNKDSLWQKL STEFRKNTTD LTYDTWIKPV TPVDFDGSTL
     TLSLPSELHR DYWKEQLAPN LIEYAFVITK GNIEPKFILD SDIKKEAQKK EPAKADSTAD
     DQDETFSFSK ETHLNPNYTF DNFIIGKGNQ MAHAAALIVS EEPGKLYNPL FFYGGVGLGK
     THLMQAIGNK RLEDHPETNV KYVTSEAFTN DFINAIQTNR TEEFRREYRN VDLLMVDDIQ
     FFAQKEGTQE EFFHTFNDLY NNDKQIVLTS DRVPQEIPKL QERLVSRFAW GLPVDITPPD
     LETRIAILKS KAKLDNLTIP NETLSYIAGQ INSNVRELEG ALSRVQAYSK LKNEPITTDL
     VYEALKGLKL AKANNELSIM DIQNKVASYF HVTISDLKGK KRMKSIVIPR QIAMYLSREM
     TSNSLPKIGK EFGGKDHTTV IHACDKIAEV IKIDADIRKE ISDIKTALS
//
DBGET integrated database retrieval system