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Database: UniProt
Entry: U4KJL8_ACHPJ
LinkDB: U4KJL8_ACHPJ
Original site: U4KJL8_ACHPJ 
ID   U4KJL8_ACHPJ            Unreviewed;       448 AA.
AC   U4KJL8;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-SEP-2017, entry version 31.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:CCV63578.1};
GN   ORFNames=BN85400010 {ECO:0000313|EMBL:CCV63578.1};
OS   Acholeplasma palmae (strain ATCC 49389 / J233).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Acholeplasma.
OX   NCBI_TaxID=1318466 {ECO:0000313|EMBL:CCV63578.1, ECO:0000313|Proteomes:UP000032740};
RN   [1] {ECO:0000313|EMBL:CCV63578.1, ECO:0000313|Proteomes:UP000032740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J233 {ECO:0000313|EMBL:CCV63578.1,
RC   ECO:0000313|Proteomes:UP000032740};
RX   PubMed=24158107; DOI=10.1159/000354322;
RA   Kube M., Siewert C., Migdoll A.M., Duduk B., Holz S., Rabus R.,
RA   Seemuller E., Mitrovic J., Muller I., Buttner C., Reinhardt R.;
RT   "Analysis of the Complete Genomes of Acholeplasma brassicae , A.
RT   palmae and A. laidlawii and Their Comparison to the Obligate Parasites
RT   from ' Candidatus Phytoplasma'.";
RL   J. Mol. Microbiol. Biotechnol. 24:19-36(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:SAAS00724167}.
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; FO681347; CCV63578.1; -; Genomic_DNA.
DR   RefSeq; WP_026653733.1; NC_022538.1.
DR   EnsemblBacteria; CCV63578; CCV63578; BN85400010.
DR   KEGG; apal:BN85400010; -.
DR   KO; K02313; -.
DR   Proteomes; UP000032740; Chromosome Acholeplasma palmae.
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; IPR024633; DnaA_N_dom.
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   Pfam; PF11638; DnaA_N; 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:UP000032740};
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:UP000032740}.
FT   DOMAIN      138    274       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      356    425       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     146    153       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   448 AA;  51735 MW;  F401C55C1395D1D5 CRC64;
     MNIYDDLWNK ILKDLEYIYS EEVYNEIFAP IKSTHKFQNG LIFIIVESEF IKNRISRMYM
     PKINELATKH FDQAVRFKFV TAQDLISEDS PKDRVLTINT YRPGNLNNAY SFDNFVVGKS
     NTFAFRMAMK VADQPGVVAN PFYIFGDVGL GKTHLMQAIG NYILDNDVNQ RVLYVKADGF
     IEDFTNLLRK EKMDDFNHKY RDIDVLLVDD IQIMAGANRT QMEFFKLFDY LYLNNKQIII
     TSDKPASELK NIMSRLTSRF EAGLTVDIQV PDLDHRLTIL KRKLSSFDPN NDVSDDVLEF
     IASSFVTNIR EMEGALIRLL SYASACNLDI TLDVAYEALD PLLKTKKRSN NLNENNYDKI
     QSVVSEFYNI SLQDLIGKKR HSKYTLPRHI AMYLIKLKYN IPYKTIGTLF SDRDHSTVLA
     ACEKIENELR QDANLKIAVD TIVKKVDA
//
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