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Database: UniProt
Entry: G0H9N5_CORVD
LinkDB: G0H9N5_CORVD
Original site: G0H9N5_CORVD 
ID   G0H9N5_CORVD            Unreviewed;       564 AA.
AC   G0H9N5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   05-JUL-2017, entry version 43.
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:AEK35347.1};
GN   OrderedLocusNames=CVAR_0001 {ECO:0000313|EMBL:AEK35347.1};
OS   Corynebacterium variabile (strain DSM 44702 / JCM 12073 / NCIMB 30131)
OS   (Corynebacterium mooreparkense).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK35347.1, ECO:0000313|Proteomes:UP000006659};
RN   [1] {ECO:0000313|EMBL:AEK35347.1, ECO:0000313|Proteomes:UP000006659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC   {ECO:0000313|Proteomes:UP000006659};
RX   PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA   Schroeder J., Maus I., Trost E., Tauch A.;
RT   "Complete genome sequence of Corynebacterium variabile DSM 44702
RT   isolated from the surface of smear-ripened cheeses and insights into
RT   cheese ripening and flavor generation.";
RL   BMC Genomics 12:545-545(2011).
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:SAAS00731907}.
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; CP002917; AEK35347.1; -; Genomic_DNA.
DR   RefSeq; WP_014008541.1; NC_015859.1.
DR   STRING; 858619.CVAR_0001; -.
DR   EnsemblBacteria; AEK35347; AEK35347; CVAR_0001.
DR   KEGG; cva:CVAR_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; AGKEHTQ; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000006659; Chromosome.
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; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
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   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:UP000006659};
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:UP000006659}.
FT   DOMAIN      255    385       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      467    536       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     263    270       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   564 AA;  61885 MW;  D54B0266A7901134 CRC64;
     MTTAEDFPTV WANLVTRWVT SDAASAEFPE VTPRSRSLLQ QLDPVVLVNG IAVLTAPSKW
     VRTETEKKLS AHISEVLERE IGMPVTLSLS VKELAAEAPA ENAPAAATAK PVEPPVQAVD
     ADEAFEEPRR SSQFGDLPSV PPGPVHTPDL WENMDDAAFP HPEFTENTQA NQPAVSSAAP
     ATAAYAEPAQ VAEPVTVTAG VPVTTAATAP AAAATHADDE NRLNPKYTFD TFVTGPSNQF
     PAAACRAVAE NPGKAYNPLF IYGQPGLGKT HLLHAIGHYA RELKPEIRVR YVSSEEMTNE
     FINAIQGGPL ALDQFKRNYR NLDLLIVDDI QFLQGKESTQ EEFFHTFNAL YQANHQIVLS
     SDRPPSQLTT LEDRLRTRFE GGLTTDVKTP DLETRMAILA KKSLLNGAAV PRDVLEFIAS
     RNESSIRELE GALTRVVAYC SMTGEPITIA AAEVVVKDIL PQDVKITPEM VIEVIADHFT
     VSIDQLTGPS KVRKIVTARQ FGMFLTREYC EMSTTKIGEV YGGRDHTTVM HAEKKMRTAI
     QENTAIFEQF QELTQKIKSR ARQR
//
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