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Database: UniProt
Entry: G7CIP3_MYCT3
LinkDB: G7CIP3_MYCT3
Original site: G7CIP3_MYCT3 
ID   G7CIP3_MYCT3            Unreviewed;       508 AA.
AC   G7CIP3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   05-JUL-2017, entry version 38.
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:EHI11372.1};
GN   ORFNames=KEK_10773 {ECO:0000313|EMBL:EHI11372.1};
OS   Mycobacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP
OS   105390 / JCM 6362 / NCTC 10409 / 316).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1078020 {ECO:0000313|EMBL:EHI11372.1, ECO:0000313|Proteomes:UP000004915};
RN   [1] {ECO:0000313|EMBL:EHI11372.1, ECO:0000313|Proteomes:UP000004915}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 /
RC   316 {ECO:0000313|Proteomes:UP000004915};
RG   Tuberculosis Structural Genomics Consortium;
RA   Ioerger T.R.;
RL   Submitted (NOV-2011) 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: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}.
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:EHI11372.1}.
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DR   EMBL; AGVE01000046; EHI11372.1; -; Genomic_DNA.
DR   RefSeq; WP_003925638.1; NZ_AGVE01000046.1.
DR   EnsemblBacteria; EHI11372; EHI11372; KEK_10773.
DR   PATRIC; fig|1078020.3.peg.2111; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000004915; Unassembled WGS sequence.
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; 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: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.
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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004915};
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:UP000004915}.
FT   DOMAIN      201    329       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      413    481       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     209    216       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   508 AA;  56972 MW;  0E95C1D60F6B4457 CRC64;
     MTADPDAPFV AVWNSVVAEL NGELDSPDSG GDPNRQPLTP QQRAWLKLVE PLVITEGFAL
     LSVPTPFVQN EIERHLREPI INALSRRLGQ RVELGVRIAT PPPQPADDPL VDTAHPQVTV
     EPRGGSRVDP DDVDEDREAR ASAEAGWPGR YFGDRPSSST DGDANGATLN RRYTFETFVI
     GASNRFAHAA TLAIAEAPAR AYNPLFIWGE SGLGKTHLLH AAGNYAQRLF PGMRVKYVST
     EEFTNDFINS LRDDRKASFK RSYRDIDILL IDDIQFIEGK EGIQEEFFHT FNTLHNANKQ
     IVISSDRPPK QLATLEDRLR TRFEWGLITD VQPPELETRI AILRKKAQMD RLDVPDDVLE
     LIASAIERNI RELEGALIRV TAFASLNKTP IDRSLAEIVL RDLISDASTM QISAAAIMAA
     TAEYFGTTVE ELRGPGKTRA LAQSRQIAMY LCRELTDLSL PRIGQAFDRD HTTVMYAEKK
     IRAEMAERRE VFDHVKELTT RIRQRAKR
//
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