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Database: UniProt
Entry: C4LGB0_CORK4
LinkDB: C4LGB0_CORK4
Original site: C4LGB0_CORK4 
ID   C4LGB0_CORK4            Unreviewed;       605 AA.
AC   C4LGB0;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   25-OCT-2017, entry version 71.
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:ACR16800.1};
GN   OrderedLocusNames=ckrop_0000 {ECO:0000313|EMBL:ACR16800.1};
OS   Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP
OS   105744 / CCUG 35717).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=645127 {ECO:0000313|EMBL:ACR16800.1, ECO:0000313|Proteomes:UP000001473};
RN   [1] {ECO:0000313|EMBL:ACR16800.1, ECO:0000313|Proteomes:UP000001473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717
RC   {ECO:0000313|Proteomes:UP000001473};
RX   PubMed=18430482; DOI=10.1016/j.jbiotec.2008.03.004;
RA   Tauch A., Schneider J., Szczepanowski R., Tilker A., Viehoever P.,
RA   Gartemann K.-H., Arnold W., Blom J., Brinkrolf K., Brune I.,
RA   Goetker S., Weisshaar B., Goesmann A., Droege M., Puehler A.;
RT   "Ultrafast pyrosequencing of Corynebacterium kroppenstedtii DSM44385
RT   revealed insights into the physiology of a lipophilic corynebacterium
RT   that lacks mycolic acids.";
RL   J. Biotechnol. 136:22-30(2008).
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}.
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DR   EMBL; CP001620; ACR16800.1; -; Genomic_DNA.
DR   RefSeq; WP_012730688.1; NC_012704.1.
DR   ProteinModelPortal; C4LGB0; -.
DR   STRING; 645127.ckrop_0000; -.
DR   EnsemblBacteria; ACR16800; ACR16800; ckrop_0000.
DR   KEGG; ckp:ckrop_0000; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; ATHIERN; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000001473; 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; 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:UP000001473};
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:UP000001473}.
FT   DOMAIN      299    430       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      510    579       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     307    314       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   605 AA;  67428 MW;  7E20F4F8561F6F79 CRC64;
     MDLGGSPHQF GQASEDFFNT WNNVVAQLMA MNPREDIPGQ APGTRITPQD KAWLKQAAPV
     GLIGGVAVIS TPNRTAKSVF ERKLGDIISA ELTAAIGEPI KLAISINSAA TETDDSSAEP
     PRTEPPRAET PPTQPRTTQS RPTETRSAES YHDFSQLNTG PKTGTPSENV AQQNTQPSHE
     MPRPTSYEDD PYVLQYPDSS PQGERPSTYP DATPTEPAYS NSGDAHVGNS YDTPAETAPQ
     PWNEGYINNA RPQRRQEQKP DSERSWLNEN YTFDNLVAGE GNRVVRAAAI AVAENPAQAY
     NPLFIWGGSG LGKTHILHAI GHRALELRPN LRVRYVSIEE YTNEWINSIR NNRGEDFKRK
     YRSFDILLVD DIQFLAGKPE TQIEFFHNFN ALHGAQKQIV LCSDRSPKEL TELEPRLRTR
     FQWGFTQDIQ KPDLETRIAI LRLKAERENA QVPSEVLSFI AEQKAESVRE LEGALNKVLI
     VSSIQHTPVT LEMARDQLQD LVAPEVVEIT APTIMSVTAE YFNLTTADLT GPGKARPIAH
     ARQVAMYLCR ELTDLSLPKV GNKFGGRDHT TAMYAERKIR KEMSEKRSTN EAIQEITARI
     KDQAR
//
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