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Database: UniProt
Entry: A0A099UG74_9HELI
LinkDB: A0A099UG74_9HELI
Original site: A0A099UG74_9HELI 
ID   A0A099UG74_9HELI        Unreviewed;       432 AA.
AC   A0A099UG74;
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, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=LS72_03710 {ECO:0000313|EMBL:KGL18748.1};
OS   Helicobacter apodemus.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=135569 {ECO:0000313|EMBL:KGL18748.1, ECO:0000313|Proteomes:UP000029920};
RN   [1] {ECO:0000313|EMBL:KGL18748.1, ECO:0000313|Proteomes:UP000029920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT-03-7007 {ECO:0000313|EMBL:KGL18748.1,
RC   ECO:0000313|Proteomes:UP000029920};
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: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}.
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:KGL18748.1}.
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DR   EMBL; JRPC01000029; KGL18748.1; -; Genomic_DNA.
DR   RefSeq; WP_034553579.1; NZ_JRPC01000029.1.
DR   EnsemblBacteria; KGL18748; KGL18748; LS72_03710.
DR   Proteomes; UP000029920; 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; 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:UP000029920};
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:UP000029920}.
FT   DOMAIN      129    259       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      339    408       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     137    144       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   432 AA;  49573 MW;  12B7B7E67165D9FB CRC64;
     MHPILLQLKK EISPFEFENY ISQIIYNEKY SRDDRIIFNA PNIFIASFIR TKYIHKITHL
     FEIQNGFKPE VIIEVYNQTA KKAITNNQKK INVATNLNPS LTFNSFIVGN SNSFAFNVAK
     AVAQNQGASY NPLVIYGNTG LGKTHLLNAI GNANASVGKI VIYTTSEQFL NDYLLHIRNN
     SMERFRQKYR ACDYLLIDDI QFLSGKNQIQ EEFFHTFNEL KENYKQIVLT SDRPPKNMDG
     LEERLKTRFT SGLLADIQPP ELETKINIIN AKCELDGIIL NPEVINFIAA NINDNIREIE
     GVLVKLNFSI NVTNIQEVTI DFVKDILKEY IKESKENINL EGIIETVSKY FNIKPSEIRS
     KSRSKNIVIA RKIVIYLART LTPNSMPYLA NFFGMKDHST ISKAMKSIQD EINKNGNLKT
     IIEELKNKIK QN
//
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