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Database: UniProt
Entry: B6BGY7_SULGG
LinkDB: B6BGY7_SULGG
Original site: B6BGY7_SULGG 
ID   B6BGY7_SULGG            Unreviewed;       435 AA.
AC   B6BGY7; H1FZF7;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   05-JUL-2017, entry version 62.
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   ECO:0000313|EMBL:EHP29771.1};
GN   ORFNames=SMGD1_1247 {ECO:0000313|EMBL:EHP29771.1};
OS   Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Sulfurimonas.
OX   NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP29771.1, ECO:0000313|Proteomes:UP000006431};
RN   [1] {ECO:0000313|EMBL:EHP29771.1, ECO:0000313|Proteomes:UP000006431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GD1 {ECO:0000313|EMBL:EHP29771.1};
RX   PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA   Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G.,
RA   Teeling H., Labrenz M., Jurgens K.;
RT   "Genome and physiology of a model Epsilonproteobacterium responsible
RT   for sulfide detoxification in marine oxygen depletion zones.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012).
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}.
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}.
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:EHP29771.1}.
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DR   EMBL; AFRZ01000001; EHP29771.1; -; Genomic_DNA.
DR   RefSeq; WP_008336544.1; NZ_DS995286.1.
DR   ProteinModelPortal; B6BGY7; -.
DR   EnsemblBacteria; EHP29771; EHP29771; SMGD1_1247.
DR   PATRIC; fig|929558.5.peg.1239; -.
DR   Proteomes; UP000006431; Unassembled WGS sequence.
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; 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.
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:UP000006431};
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:UP000006431}.
FT   DOMAIN      132    258       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      341    410       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     140    147       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   435 AA;  49739 MW;  7A82E7F2E8A27847 CRC64;
     MNIGQEVLEL LKEEITEVQY NRYIKQLIYD AKKSTSDLAI FYAPNALVNN WIKSKYSEKI
     AHLFEVKSGS KVSVKITLKN STDKRIKLQK TEQKLQHSLL NPSHTFDNFM VGGSNQFAYA
     AVKSVSESPG EVYNPLFIYG GVGLGKTHLM QSAGNVFQNQ GKSVIYTSVE QFLNDFIRHV
     RNKTMPSFQE KYRKCDVLLI DDIQFLSNKE GIQEEFFHTF EALKGSGKQI ILTADKHPKK
     IGGLEKRLQS RFEWGLVADI QPPELETKIA IIKKKCEINK VKLSNDIINY IATVIESNVR
     EIEGILSKLH AYSQLMHIDI DLAFTKNVLK DQLQENRANL TLDVITNNVA KDLNIKPTEI
     RSKGRSKNLV YARRISIYLC RELTQNTMPQ LAQYFGMKDH TAISHTLKKI NELMKNDEDF
     KVKIEELTNK ITSVS
//
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