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Database: UniProt
Entry: A0A0C2YSS0_9PROT
LinkDB: A0A0C2YSS0_9PROT
Original site: A0A0C2YSS0_9PROT 
ID   A0A0C2YSS0_9PROT        Unreviewed;       439 AA.
AC   A0A0C2YSS0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   25-OCT-2017, entry version 22.
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=KN64_14400 {ECO:0000313|EMBL:KIM02710.1};
OS   Sulfurovum sp. AS07-7.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Sulfurovum.
OX   NCBI_TaxID=1539062 {ECO:0000313|EMBL:KIM02710.1, ECO:0000313|Proteomes:UP000031941};
RN   [1] {ECO:0000313|EMBL:KIM02710.1, ECO:0000313|Proteomes:UP000031941}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=25620962; DOI=10.3389/fmicb.2014.00756;
RA   Hamilton T.L., Jones D.S., Schaperdoth I., Macalady J.L.;
RT   "Metagenomic insights into S(0) precipitation in a terrestrial
RT   subsurface lithoautotrophic ecosystem.";
RL   Front. Microbiol. 5:756-756(2014).
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:SAAS00911680}.
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:KIM02710.1}.
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DR   EMBL; JQIP01000074; KIM02710.1; -; Genomic_DNA.
DR   EnsemblBacteria; KIM02710; KIM02710; KN64_14400.
DR   Proteomes; UP000031941; 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   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: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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031941};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031941}.
FT   DOMAIN      135    261       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      344    413       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     143    150       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   439 AA;  50603 MW;  4D1E5BBBB12BB23D CRC64;
     MSLGQKVLDE LKKEISQNDY EKYIKKLLFD EKRSRSDLAC FHAPNIIIAK WVKTKYESQI
     THLFELQTGI KPELIIDIKN EKNTAFSIKK QQTEKTPQKA NFLNPSLTFD NFIVGSSNQF
     AYTAAKSVSE KPGQLYNPLF LYGGVGLGKT HLLQAIGNVA ISQGKNVVYT TLETFMNTFT
     SHIRNQTMDR FREKFRKCDL LLIDDIQFIS RKEQTQEEFF HTFNELFNAK KQIVLTADKP
     PNKIAGLADR LKSRFEWGLM ADIQPPELET KIEIIKKKCQ LDKIHLTNDV INFIATNMGD
     NIREIEGTII KLNALSSILN QKITLEFAKN SIKDQLKEKK ENITIEYISQ IVARELNIKP
     SDIKSKKRTQ NIVNARRIII YLARNLTPNS MPQIALYFGM KDHTAISHAM KKINEMIDND
     ENLKVFLEEI SNKINSKDY
//
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