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Database: UniProt
Entry: A0A0I9V0Y7_9MYCO
LinkDB: A0A0I9V0Y7_9MYCO
Original site: A0A0I9V0Y7_9MYCO 
ID   A0A0I9V0Y7_9MYCO        Unreviewed;       508 AA.
AC   A0A0I9V0Y7;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   25-OCT-2017, entry version 18.
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   ORFNames=ABH38_15625 {ECO:0000313|EMBL:KLO35514.1};
OS   Mycobacterium haemophilum.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=29311 {ECO:0000313|EMBL:KLO35514.1, ECO:0000313|Proteomes:UP000036334};
RN   [1] {ECO:0000313|EMBL:KLO35514.1, ECO:0000313|Proteomes:UP000036334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UC1 {ECO:0000313|Proteomes:UP000036334};
RA   Greninger A.L., Cunningham G., Miller S.;
RT   "Genome sequence of Mycobacterium haemophilum.";
RL   Submitted (MAY-2015) 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   -!- 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:KLO35514.1}.
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DR   EMBL; LDPR01000014; KLO35514.1; -; Genomic_DNA.
DR   RefSeq; WP_047315659.1; NZ_LDPT01000017.1.
DR   EnsemblBacteria; KLO35514; KLO35514; ABH38_15625.
DR   PATRIC; fig|29311.18.peg.1296; -.
DR   Proteomes; UP000036334; 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; 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:UP000036334};
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:UP000036334}.
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;  56682 MW;  5E66E514BFDBE217 CRC64;
     MTDDPGLGFT TVWNAVVSEL NGESNADDGA TNDNALVTPL TPQQRAWLNL VQPLTIVEGF
     ALLSVPSSFV QNEIERHLRT PITDALSRRL GQQIQLGVRI APPAADNVDD NFPPAESIPP
     AEVLPADDCG TDTDENYGEP LADGHQGWPA YFTERPRHAE SAAAGGTSLN RRYTFETFVI
     GASNRFAHAA ALAIAEAPAR AYNPLFIWGE SGLGKTHLLH AAGNYAQRLF PGMRVKYVST
     EEFTNDFINS LRDDRKVAFK RSYRDVDVLL VDDIQFIEGK EGIQEEFFHT FNTLHNANKQ
     IVISSDRPPK QLATLEDRLR TRFEWGLITD VQPPELETRI AILRKKAQME RLAVPDDVLE
     LIASSIERNI RELEGALIRV TAFASLNKTP IDKALAEIVL RDLIADASTM QISSATIMAA
     TAEYFDTTIE ELRGPGKTRA LAQSRQIAMY LCRELTDLSL PKIGQAFGRD HTTVMYAQRK
     ILSEMAERRE VFDHVKELTT RIRQRSKR
//
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