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Database: UniProt
Entry: A0A165XZN7_9BACI
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ID   A0A165XZN7_9BACI        Unreviewed;       454 AA.
AC   A0A165XZN7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   05-JUL-2017, entry version 10.
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=AZI98_07925 {ECO:0000313|EMBL:KZN96568.1};
OS   Aeribacillus pallidus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Aeribacillus.
OX   NCBI_TaxID=33936 {ECO:0000313|EMBL:KZN96568.1, ECO:0000313|Proteomes:UP000076476};
RN   [1] {ECO:0000313|EMBL:KZN96568.1, ECO:0000313|Proteomes:UP000076476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8m3 {ECO:0000313|EMBL:KZN96568.1,
RC   ECO:0000313|Proteomes:UP000076476};
RA   Poltaraus A.B., Nazina T.N., Tourova T.P., Malakho S.M.,
RA   Korshunova A.V., Sokolova D.S.;
RT   "Draft genome sequence of Aeribacillus pallidus 8m3 from petroleum
RT   reservoir.";
RL   Submitted (APR-2016) 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:KZN96568.1}.
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DR   EMBL; LWBR01000019; KZN96568.1; -; Genomic_DNA.
DR   RefSeq; WP_063387746.1; NZ_LWBR01000019.1.
DR   EnsemblBacteria; KZN96568; KZN96568; AZI98_07925.
DR   Proteomes; UP000076476; 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:UP000076476};
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:UP000076476}.
FT   DOMAIN      145    273       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      357    426       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     153    160       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   454 AA;  51842 MW;  04AA45A8D2788A8C CRC64;
     MENIEDLWNR VLAEIKKKVS KPSFDTWLKS TKAHALQGDL LIITAPNEFA RDWLESRYLH
     LIANTIYDLT GEEIGIKFII PQNLTDDEFM PKAPIKTSPK KGEETNEFPQ NLLNPKYTFD
     TFVIGSGNRF AHAASLAVAE APAKAYNPLF IYGGVGLGKT HLMHAIGHYV LEHNPSARVV
     YLSSEKFTNE FINSIRDNKA DEFRNKYRNV DVLLIDDIQF LAGKEQTQEE FFHTFNTLHE
     ESKQIVISSD RPPKEIPTLE DRLRSRFEWG LITDITPPDL ETRIAILRKK AKADGLDIPN
     EVMLYIANQI DTNIRELEGA LIRVVAYSSL INKDINADLA AEALKDIIPS SKPKIITIQE
     IQRVVGQHFN VKLEDFKAKK RTKSVAFPRQ IAMYLSRELT DSSLPKIGEE FGGRDHTTVI
     HAHEKISKLL EEDPQLQNQI NEIKEQLKHS IHYH
//
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