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Database: UniProt
Entry: A0A060R8N0_9BACT
LinkDB: A0A060R8N0_9BACT
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ID   A0A060R8N0_9BACT        Unreviewed;       448 AA.
AC   A0A060R8N0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   25-OCT-2017, entry version 29.
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   ORFNames=BN938_0001 {ECO:0000313|EMBL:CDN30108.1};
OS   Mucinivorans hirudinis.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Mucinivorans.
OX   NCBI_TaxID=1433126 {ECO:0000313|EMBL:CDN30108.1, ECO:0000313|Proteomes:UP000027616};
RN   [1] {ECO:0000313|EMBL:CDN30108.1, ECO:0000313|Proteomes:UP000027616}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=25657285; DOI=10.1128/genomeA.01530-14;
RA   Nelson M.C., Bomar L., Graf J.;
RT   "Complete Genome Sequence of the Novel Leech Symbiont Mucinivorans
RT   hirudinis M3T.";
RL   Genome Announc. 3:e01530-e01514(2015).
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:SAAS00911680}.
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; HG934468; CDN30108.1; -; Genomic_DNA.
DR   RefSeq; WP_038656938.1; NZ_HG934468.1.
DR   EnsemblBacteria; CDN30108; CDN30108; BN938_0001.
DR   KEGG; rbc:BN938_0001; -.
DR   PATRIC; fig|1433126.3.peg.1; -.
DR   KO; K02313; -.
DR   Proteomes; UP000027616; Chromosome I.
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:SF2; PTHR30050:SF2; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000027616};
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:UP000027616}.
FT   DOMAIN      146    276       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      357    426       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     154    161       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   448 AA;  50875 MW;  B89D354D937950F4 CRC64;
     MWQQCLVQIR KSLSEDDFVR WFKHIEAVAF DGAVLKLQVP NQEHYKYIEQ NFIPILRPIV
     RNVFGVKARV TYSIPKPSAE QQARGYATEP DRQTIKNPFV IPGIKKVQFD SQLQPELTFR
     NHIEGDCNRL ARSAGISISI NPGTTSFNPL FIYGNSGLGK THIAQAVGNA TKERHPDSKV
     LYVSANHFQS QFQTAAWRGE LNDFIHFYQM IDVLIIDDIQ EFAGKPGTQN IFFNIFNHLR
     LLGKQIILTS DRPPVELKDI EDRLITRFKW GLSAGLTPPD HQTKVSILQA KCSRMGLILG
     ADIIDFLAEN IKANIRELEG ALTSLEAHSS LLGKEISFEL AHRIMQDIVK ISSKEVNIDL
     IMDLVSEQMK ISRTQLLSKE RTREVATARQ VVMYLCKQHT KTPLTVIGAA IGGRNHATVL
     HAHKNIINMI DTDRSLRKHI EEMERKLL
//
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