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Database: UniProt
Entry: K8DZ67_9FIRM
LinkDB: K8DZ67_9FIRM
Original site: K8DZ67_9FIRM 
ID   K8DZ67_9FIRM            Unreviewed;       441 AA.
AC   K8DZ67;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   25-OCT-2017, entry version 36.
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:CCO08317.1};
GN   ORFNames=DESHY_30007 {ECO:0000313|EMBL:CCO08317.1};
OS   Desulfotomaculum hydrothermale Lam5 = DSM 18033.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO08317.1, ECO:0000313|Proteomes:UP000009315};
RN   [1] {ECO:0000313|EMBL:CCO08317.1, ECO:0000313|Proteomes:UP000009315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RA   Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V.,
RA   Medigue C., Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT   "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT   hydrothermale Lam5(T).";
RL   Genome Announc. 1:e00114-e00112(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: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:CCO08317.1}.
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DR   EMBL; CAOS01000010; CCO08317.1; -; Genomic_DNA.
DR   RefSeq; WP_008411692.1; NZ_FQXF01000038.1.
DR   EnsemblBacteria; CCO08317; CCO08317; DESHY_30007.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000009315; 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; 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:UP000009315};
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:UP000009315}.
FT   NP_BIND     144    151       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   441 AA;  50654 MW;  F06575D6892BE6F6 CRC64;
     MQSDILARWE QVLIRLEKQV NKHSFETWLA RCKPVAHYDN TIIIEVPDHF SKGWLADRYA
     PLIKQAYESI LHREISLQFI LAGQEVDQPK PKERLQEDTY INILNPRYTF DTFVIGNSNR
     FAHAASLAVA ESPAKAYNPL FIYGGVGLGK THLMHAIGHY ILENNPRLKV AYVTSEKFTN
     ELINSIRDDQ TVEFRNKYRS MDILLIDDIQ FLEKKERTQE EFFHTFNTLY EANKQIIISS
     DRPPKEIATL EDRLRSRFEW GLITDIQPPD YETRVAILRK KAQLEGISNI PDETIAFIAD
     KIHSNIRELE GALIRVSAFS SLEKREATPH LAAEVLKDVI SPSKPKVITV SLIMQCVADF
     YGLRIDDLKA KKRTRSVAFP RQVAMYLTRE LTDLSLPKIG DEFGGRDHTT VLHACEKIVA
     DLPGDPVLQE TIKELKKRIS E
//
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