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Database: UniProt
Entry: E7G2M2_9HELI
LinkDB: E7G2M2_9HELI
Original site: E7G2M2_9HELI 
ID   E7G2M2_9HELI            Unreviewed;       433 AA.
AC   E7G2M2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   05-JUL-2017, entry version 38.
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:EFX42371.1};
GN   ORFNames=HSUHS5_0162 {ECO:0000313|EMBL:EFX42371.1};
OS   Helicobacter suis HS5.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=710394 {ECO:0000313|EMBL:EFX42371.1, ECO:0000313|Proteomes:UP000054093};
RN   [1] {ECO:0000313|EMBL:EFX42371.1, ECO:0000313|Proteomes:UP000054093}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS5 {ECO:0000313|EMBL:EFX42371.1,
RC   ECO:0000313|Proteomes:UP000054093};
RX   PubMed=21414191; DOI=10.1186/1297-9716-42-51;
RA   Vermoote M., Vandekerckhove T.T., Flahou B., Pasmans F., Smet A.,
RA   De Groote D., Van Criekinge W., Ducatelle R., Haesebrouck F.;
RT   "Genome sequence of Helicobacter suis supports its role in gastric
RT   pathology.";
RL   Vet. Res. 42:51-51(2011).
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:EFX42371.1}.
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DR   EMBL; ADHO01000028; EFX42371.1; -; Genomic_DNA.
DR   RefSeq; WP_006564372.1; NZ_ADHO01000028.1.
DR   EnsemblBacteria; EFX42371; EFX42371; HSUHS5_0162.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000054093; 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   Complete proteome {ECO:0000313|Proteomes:UP000054093};
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:UP000054093}.
FT   DOMAIN      129    259       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      338    407       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     137    144       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   433 AA;  48883 MW;  9AE49BB7F446F733 CRC64;
     MLEAILETLK ADLSEFEFKT YVEILRFDEK ASRADCFVFY APNIWVCNYI KTRYSTLLEN
     AIGAYKGYPV SVEVLPREQQ IKNSPLKPLC QAHQNPSLNP AFTFDTLVVG SCNHLAIKVA
     SQVAQNSGSY NPVLFFGGVG LGKTHILNAI GNKACDRLQD VLYVTAEQFL NDYVFRLGNH
     SMDKFQDKYR TRDYLLIDDV QFFGGKQMVQ EEFFHTFNAL HSQGSQIVMT SDKPPRDIKG
     LADRLLSRFE MGMIASIQPP KLETKIAIIN QKCQFNHIRM DAPVVEYLAS HTNENIRQIE
     GALLRLNATA MLTGVSIDLS LVEAVLKDTI KESLQEVSLE QVLRVVAKTL NLKPSDIRNN
     YRNRQVALAR KLIIYLARIL TNASTTALAQ FLGMKDHSGV SKANKTVTKC MLEDKHTKLL
     IEEMRAKILS HVD
//
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