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Database: UniProt
Entry: A0A0C2ZJ14_9PROT
LinkDB: A0A0C2ZJ14_9PROT
Original site: A0A0C2ZJ14_9PROT 
ID   A0A0C2ZJ14_9PROT        Unreviewed;       447 AA.
AC   A0A0C2ZJ14;
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=KU28_06480 {ECO:0000313|EMBL:KIM07569.1};
OS   Sulfurovum sp. PC08-66.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Sulfurovum.
OX   NCBI_TaxID=1539063 {ECO:0000313|EMBL:KIM07569.1, ECO:0000313|Proteomes:UP000031940};
RN   [1] {ECO:0000313|EMBL:KIM07569.1, ECO:0000313|Proteomes:UP000031940}
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:KIM07569.1}.
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DR   EMBL; JQIQ01000015; KIM07569.1; -; Genomic_DNA.
DR   EnsemblBacteria; KIM07569; KIM07569; KU28_06480.
DR   Proteomes; UP000031940; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031940};
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:UP000031940}.
FT   DOMAIN      140    266       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      349    418       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     148    155       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      418    447       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   447 AA;  51108 MW;  8C518436A66D020A CRC64;
     MNLGQKILLE LKKEISLSDY DRYIKPLSYD IDNSRSNISY YYAPNLLVAK WIRTKFSDKI
     AHLFELQSGI RPKIKIEVKK NKSHTQSAPS GEIADNSAKR ISSKSTILNP SFTFESFIVG
     SSNQFAFTTA QSVAQKPGRQ YNPLFLYGGV GLGKTHLLQA IGNYHLHLGK KVIYTTLEQF
     MNKFTSHLRS QSMDRFRDHF RECDLLLIDD VQFLSRKEQT QEEFFHTFNE LHTANKQIVI
     TADRPPNKIA GLVDRLKSRF EWGLLADIQP PGLETKIAII QKKCELDGIV LNNDVVNYIA
     SNMGSNIREI EGTIIKLNAM SSILNQEITL EFTQNAIRDQ LQDKKESLNI DDIVNFIATE
     LNVKPADIKS KKRNKNIVNA RRISIYLARN LTTSSMPQIA VYFGMKDHTA ISHSMRKINE
     IVENDDNFKL LLEELENKIS ANKIKFD
//
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