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Database: UniProt
Entry: A0A099BBQ5_9HELI
LinkDB: A0A099BBQ5_9HELI
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ID   A0A099BBQ5_9HELI        Unreviewed;       437 AA.
AC   A0A099BBQ5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   05-JUL-2017, entry version 23.
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   ORFNames=LS64_03555 {ECO:0000313|EMBL:KGI52963.1};
OS   Helicobacter saguini.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1548018 {ECO:0000313|EMBL:KGI52963.1, ECO:0000313|Proteomes:UP000029714};
RN   [1] {ECO:0000313|EMBL:KGI52963.1, ECO:0000313|Proteomes:UP000029714}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 97-6194 {ECO:0000313|EMBL:KGI52963.1,
RC   ECO:0000313|Proteomes:UP000029714};
RA   Sheh A., Shen Z., Fox J.G.;
RT   "Genome sequencing of Helicobacter and Campylobacter species isolated
RT   from rodents.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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:SAAS00731907}.
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:KGI52963.1}.
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DR   EMBL; JRMP01000174; KGI52963.1; -; Genomic_DNA.
DR   RefSeq; WP_034570703.1; NZ_JRMP01000174.1.
DR   EnsemblBacteria; KGI52963; KGI52963; LS64_03555.
DR   Proteomes; UP000029714; 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; 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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029714};
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:UP000029714}.
FT   DOMAIN      132    264       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      342    412       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     140    147       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      412    437       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   437 AA;  50528 MW;  29219D6E603E2249 CRC64;
     MNGNDVLEIL RENSSMLEKT QYLDKIAYDY NKSSESKFIF IAKNSFILNW VKRKYESKML
     EIAQNAHITP KIIFILESQL NIETIDDVKT RYYIKNNTAM TNTECSFENF IVGECNAFAY
     ESAKSVVDSK ARYNPLLIHG STGLGKTHLL HSICNAVYKK NPNASVIYIE AETMFNEYKH
     RITNKSMDQF RERFRKCDYL LIDDVQFLGV SEKFQEEFFN TFNNIVQEGG QIVMTSDKPP
     KKIEKLETRL KSRFMGGMMA KIESPELETR INIIKQKCRV RNIQLDSEVI EFIAVKIQEN
     IRDLEGTITT IYGNMMLLKV PITIELLKTI LEDRSTQSHE INLNDIINLM ALEYNIKPSE
     IKSKTRGKKN VAKARKIVAY LAKNVTRTSF PDIAMELNLK GHSAVSKQIK TISDEIQKDS
     KLKMEIENLK NKLMQKN
//
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