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Database: UniProt
Entry: A0A268TXN2_9HELI
LinkDB: A0A268TXN2_9HELI
Original site: A0A268TXN2_9HELI 
ID   A0A268TXN2_9HELI        Unreviewed;       440 AA.
AC   A0A268TXN2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   16-JAN-2019, entry version 9.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=BKH41_01780 {ECO:0000313|EMBL:PAF49422.1};
OS   Helicobacter sp. 12S02232-10.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1476197 {ECO:0000313|EMBL:PAF49422.1, ECO:0000313|Proteomes:UP000216724};
RN   [1] {ECO:0000313|EMBL:PAF49422.1, ECO:0000313|Proteomes:UP000216724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12S02232-10 {ECO:0000313|EMBL:PAF49422.1,
RC   ECO:0000313|Proteomes:UP000216724};
RX   PubMed=28827684; DOI=.1038/s41598-017-09091-7;
RA   Gilbert M.J., Duim B., Timmerman A.J., Zomer A.L., Wagenaar J.A.;
RT   "Whole genome-based phylogeny of reptile-associated Helicobacter
RT   indicates independent niche adaptation followed by diversification in
RT   a poikilothermic host.";
RL   Sci. Rep. 7:8387-8387(2017).
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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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:PAF49422.1}.
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DR   EMBL; MLAQ01000002; PAF49422.1; -; Genomic_DNA.
DR   Proteomes; UP000216724; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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:SAAS00756129};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000216724};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117}.
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}.
FT   COILED      417    437       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   440 AA;  50717 MW;  348B46C23454BD5E CRC64;
     MLENDILKQL KDEITEYEYN TYISKMKYDE NTSKSDLAVF IVPNIYIANW IKTKYSEKII
     HLFEIYKKIK PEISIIVESQ KKDVKSSKNY GSKLQTRAIL NPSYTFDSFV VGDSNRFCYE
     IAKKISQRQA EVYNPVLIYG GTGLGKTHIL NAIGNSVSEK NKIVIYVTAE QFLNDFITRI
     NNNTMDRFRD KYRSCDYLLI DDVQFFGGKE GVQQEFFHTF NELHDKKKQI VMTSDKPPKQ
     ILGLEERLKS RFEWGIIADI QPPGLETKIA IIIQKCHLNQ IEIDREIIHY LASNINDNIR
     QIEGIILKLN AQASIIGQNI TLAMAKNAIK DTQKENLENI TLENIIKIVS KELNIKPSEI
     KSKSRNKTTA NARRIVIYLA RTLTPNSMPA LAQFLNMKDH SSVSKAMKMI TTEIAENINI
     KSMIEEMKNK IQNEQNNKII
//
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