GenomeNet

Database: UniProt
Entry: W5XWU2_9CORY
LinkDB: W5XWU2_9CORY
Original site: W5XWU2_9CORY 
ID   W5XWU2_9CORY            Unreviewed;       557 AA.
AC   W5XWU2;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   25-OCT-2017, entry version 30.
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:AHI21397.1};
GN   ORFNames=B843_00005 {ECO:0000313|EMBL:AHI21397.1};
OS   Corynebacterium vitaeruminis DSM 20294.
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=1224164 {ECO:0000313|EMBL:AHI21397.1, ECO:0000313|Proteomes:UP000019222};
RN   [1] {ECO:0000313|EMBL:AHI21397.1, ECO:0000313|Proteomes:UP000019222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10234 {ECO:0000313|Proteomes:UP000019222};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "The complete genome sequence of Corynebacterium vitaeruminis DSM
RT   20294.";
RL   Submitted (FEB-2013) 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:SAAS00735475}.
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP004353; AHI21397.1; -; Genomic_DNA.
DR   RefSeq; WP_025251476.1; NZ_CP004353.1.
DR   EnsemblBacteria; AHI21397; AHI21397; B843_00005.
DR   KEGG; cvt:B843_00005; -.
DR   PATRIC; fig|1224164.3.peg.1; -.
DR   KO; K02313; -.
DR   Proteomes; UP000019222; 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   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; 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.
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:UP000019222};
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:UP000019222}.
FT   DOMAIN      249    377       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      461    530       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     257    264       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   557 AA;  61798 MW;  EF8BF358FCD7B304 CRC64;
     MSDSQAPLHE TWRKVVEELF VLTSTPDSGL QPLGPQQRAY LQLVKPVALV EGVAVLAVPH
     AKAKEIIETE LGTAITQVLG MKMGRAFALA VTIDPSVSPE PVPVPAHVQA SPAPRQEAPV
     EEPRAEYRFE EPHTAGNNPF YGEQSHVTTA DSLRHQVAPE FQMSGPELTP TTATLAPQEA
     ASAGWETTHA PAAPADSGFK RNPQAAPKHA GEQPVSLNPL HTFDNYVVSD SNKLPASAAI
     AVAEKPARAY NPLFIWGDSG LGKTHLMHAI GNYAHQLHPR LKIKYVSSEE FTNDYINSVR
     DDRQESFKRR YREVDILMVD DIQFLQGKEG TQEEFFHTFN ALEQGGKQIV LSSDRPPKQL
     TTLEDRLRTR FQAGLIADIY PPDLETRIAI LSKKSRADGI ETDREVLELI ASRFDSSIRE
     LEGAFIRVSA YASVNKLELN RETAEIALRS ISPDQSNIEI TPETIIEVTA DYFQIRAQDL
     KGTTKTRNIA HARQIAMYLC RELTELSLPK IGESFGGKDH TTVMYADRKI RKDIGEKRDT
     YNEIQQITNQ IKGQGNS
//
DBGET integrated database retrieval system