GenomeNet

Database: UniProt
Entry: U5WR23_MYCKA
LinkDB: U5WR23_MYCKA
Original site: U5WR23_MYCKA 
ID   U5WR23_MYCKA            Unreviewed;       534 AA.
AC   U5WR23;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   25-OCT-2017, entry version 33.
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=MKAN_14825 {ECO:0000313|EMBL:AGZ51402.1};
OS   Mycobacterium kansasii ATCC 12478.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=557599 {ECO:0000313|EMBL:AGZ51402.1, ECO:0000313|Proteomes:UP000017786};
RN   [1] {ECO:0000313|EMBL:AGZ51402.1, ECO:0000313|Proteomes:UP000017786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12478 {ECO:0000313|EMBL:AGZ51402.1,
RC   ECO:0000313|Proteomes:UP000017786};
RG   McGill University Mycobacterium genome consortium;
RA   Veyrier F.J., Behr M.A.;
RT   "Genome sequence of Mycobacterium kansasii.";
RL   Submitted (OCT-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; CP006835; AGZ51402.1; -; Genomic_DNA.
DR   STRING; 557599.MkanA1_010100022435; -.
DR   EnsemblBacteria; AGZ51402; AGZ51402; MKAN_14825.
DR   KEGG; mkn:MKAN_14825; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000017786; 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:UP000017786};
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}.
FT   DOMAIN      227    355       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      439    507       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     235    242       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   534 AA;  59099 MW;  293E895B35A0A831 CRC64;
     MDSLLFADNC TSMSDQGDAS LTDDPGSGFA SVWNAVVSEL NGELNADGIA HTGTTLTTPL
     TPQQRAWLNL VQPLTIVEGF ALLSVPSSFV QNEIERHLRT PITDALSRRL GHQIQLGVRI
     APPPPTTDAD EGAQPADDSG LEMSRETSPE TPEAPGDTDD ADETAGGPRP GWPTYFTKRP
     SGTADTVAAT GGTSLNRRYT FDTFVIGASN RFAHAATLAI AEAPARAYNP LFIWGESGLG
     KTHLLHAAGN YTQRLFPGMR VKYVSTEEFT NDFINSLRDD RKVAFKRSYR DVDVLLVDDI
     QFIEGKEGIQ EEFFHTFNTL HNANKQIVIS SDRPPKQLAT LEDRLRTRFE WGLITDVQPP
     ELETRIAILR KKAQMERLAV PDDVLELIAS SIERNIRELE GALIRVTAFA SLNKTPIDKA
     LAEIVLRDLI ADATAMQISA ATIMAATAEY FDTTVEELRG PGKTRSLAQS RQIAMYLCRE
     LTDLSLPKIG QAFGRDHTTV MYAQRKILSE MAERREVFDH VKELTTRIRQ RSKR
//
DBGET integrated database retrieval system