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Database: UniProt
Entry: A0A0A1FMT7_9MYCO
LinkDB: A0A0A1FMT7_9MYCO
Original site: A0A0A1FMT7_9MYCO 
ID   A0A0A1FMT7_9MYCO        Unreviewed;       505 AA.
AC   A0A0A1FMT7;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   05-JUL-2017, entry version 23.
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=G155_00005 {ECO:0000313|EMBL:AIY44237.1};
OS   Mycobacterium sp. VKM Ac-1817D.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1273687 {ECO:0000313|EMBL:AIY44237.1, ECO:0000313|Proteomes:UP000030340};
RN   [1] {ECO:0000313|EMBL:AIY44237.1, ECO:0000313|Proteomes:UP000030340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-1817D {ECO:0000313|EMBL:AIY44237.1,
RC   ECO:0000313|Proteomes:UP000030340};
RX   PubMed=23474435; DOI=10.1016/j.jsbmb.2013.02.016;
RA   Bragin E.Y., Shtratnikova V.Y., Dovbnya D.V., Schelkunov M.I.,
RA   Pekov Y.A., Malakho S.G., Egorova O.V., Ivashina T.V., Sokolov S.L.,
RA   Ashapkin V.V., Donova M.V.;
RT   "Comparative analysis of genes encoding key steroid core oxidation
RT   enzymes in fast-growing Mycobacterium spp. strains.";
RL   J. Steroid Biochem. Mol. Biol. 138:41-53(2013).
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; CP009914; AIY44237.1; -; Genomic_DNA.
DR   RefSeq; WP_003883351.1; NZ_CP009914.1.
DR   EnsemblBacteria; AIY44237; AIY44237; G155_00005.
DR   GeneID; 29428426; -.
DR   KEGG; myv:G155_00005; -.
DR   KO; K02313; -.
DR   Proteomes; UP000030340; 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; 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:UP000030340};
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:UP000030340}.
FT   DOMAIN      198    326       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      410    478       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     206    213       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   505 AA;  56684 MW;  C957D4D8378D21A4 CRC64;
     MPADPDPPFV AVWNSVVAEL NGDRDSNSDP ALPPLTPQQR AWLKLVKPLV IAEGFALLSV
     PTPFVQNEIE RHLREPIINA LSRKLGQRVE LGVRIATPPE ESEDSSSDAG LSDDERPDAS
     AATPAADLDE IDDDRAAKAS AEESWPTYFS SPQRDSTISD DNAVNLNRRY TFDTFVIGAS
     NRFAHAATLA IAEAPARAYN PLFIWGESGL GKTHLLHAAG NYAQRLFPGM RVKYVSTEEF
     TNDFINSLRD DRKASFKRSY RDIDILLVDD IQFIEGKEGI QEEFFHTFNT LHNANKQIVI
     SSDRPPKQLA TLEDRLRTRF EWGLITDVQP PELETRIAIL RKKAQMDRLD VPDDVLELIA
     SSIERNIREL EGALIRVTAF ASLNKTRIDK ALAEVVLRDL IADATTMQIS TAAIMAATAE
     YFETTVEELR GPGKTRALAQ SRQIAMYLCR ELTDLSLPKI GQAFGRDHTT VMYAEKKIRG
     EMAERREVFD HVKELTTRIR QRAKR
//
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