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Database: UniProt
Entry: D3UFJ6_HELM1
LinkDB: D3UFJ6_HELM1
Original site: D3UFJ6_HELM1 
ID   D3UFJ6_HELM1            Unreviewed;       429 AA.
AC   D3UFJ6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   05-JUL-2017, entry version 54.
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:CBG39267.1};
GN   OrderedLocusNames=HMU00010 {ECO:0000313|EMBL:CBG39267.1};
OS   Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 /
OS   12198) (Campylobacter mustelae).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=679897 {ECO:0000313|EMBL:CBG39267.1, ECO:0000313|Proteomes:UP000001522};
RN   [1] {ECO:0000313|EMBL:CBG39267.1, ECO:0000313|Proteomes:UP000001522}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43772 / LMG 18044 / NCTC 12198 / 12198
RC   {ECO:0000313|Proteomes:UP000001522};
RX   PubMed=20219135; DOI=10.1186/1471-2164-11-164;
RA   O'Toole P.W., Snelling W.J., Canchaya C., Forde B.M., Hardie K.R.,
RA   Josenhans C., Graham R.L.J., McMullan G., Parkhill J., Belda E.,
RA   Bentley S.D.;
RT   "Comparative genomics and proteomics of Helicobacter mustelae, an
RT   ulcerogenic and carcinogenic gastric pathogen.";
RL   BMC Genomics 11:164-164(2010).
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; FN555004; CBG39267.1; -; Genomic_DNA.
DR   RefSeq; WP_013022368.1; NC_013949.1.
DR   STRING; 679897.HMU00010; -.
DR   EnsemblBacteria; CBG39267; CBG39267; HMU00010.
DR   KEGG; hms:HMU00010; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; VENWVKD; -.
DR   OrthoDB; POG091H02FF; -.
DR   BioCyc; HMUS679897:GJBK-1-MONOMER; -.
DR   Proteomes; UP000001522; 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; 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:UP000001522};
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:UP000001522}.
FT   DOMAIN      130    259       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      339    408       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     138    145       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   429 AA;  49043 MW;  0B7D14964693B777 CRC64;
     MTDKNLQEIF KNEFEIEEYD SIFSQIKIVE NPQNSDVVSF IAPNVYIEKW IKTKYLQRLA
     EILEKHYNIT PEIHVVTAVK KSHVKSLKQG AKKMEAALNA SYTFETFIQG DSNKFAYEIA
     KKICEKQGKA YNPVLFYGGT GLGKTHLLNA IGNKVIEKNK SVIYITSEQF LNDYSERLKS
     NTMEKFREKY RNCDYLLIDD IQFFAGKIQI QEEFFHTFNE LHLKNKQIVI TADKSLKQIL
     GLEERLKSRC EWGITADIQP PGIETKIEII KQKCIIHHVE INQDIIECLA YNIGGNIRQI
     EGIILKLNAL PLLIGQPITL SMAQNAIKDI RKEVSENIDI NAIIKATARE FNIKPSEITS
     KSRATKIAQA RRIVIYLSRE LIPHSMAMIA QSLNMKDHSA VSKAGTKINK ELKEDPALQL
     AINEIKSKL
//
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