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Database: UniProt
Entry: A0A0P6XMI0_9CHLR
LinkDB: A0A0P6XMI0_9CHLR
Original site: A0A0P6XMI0_9CHLR 
ID   A0A0P6XMI0_9CHLR        Unreviewed;       443 AA.
AC   A0A0P6XMI0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   16-JAN-2019, entry version 23.
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=AC812_03410 {ECO:0000313|EMBL:KPL77592.1};
OS   Bellilinea caldifistulae.
OC   Bacteria; Chloroflexi; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Bellilinea.
OX   NCBI_TaxID=360411 {ECO:0000313|EMBL:KPL77592.1, ECO:0000313|Proteomes:UP000050514};
RN   [1] {ECO:0000313|EMBL:KPL77592.1, ECO:0000313|Proteomes:UP000050514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GOMI-1 {ECO:0000313|EMBL:KPL77592.1,
RC   ECO:0000313|Proteomes:UP000050514};
RA   Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT   "Draft genome of Bellilinea caldifistulae DSM 17877.";
RL   Submitted (JUL-2015) 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: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:KPL77592.1}.
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DR   EMBL; LGHJ01000009; KPL77592.1; -; Genomic_DNA.
DR   RefSeq; WP_061913617.1; NZ_LGHJ01000009.1.
DR   EnsemblBacteria; KPL77592; KPL77592; AC812_03410.
DR   PATRIC; fig|360411.5.peg.3564; -.
DR   Proteomes; UP000050514; 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   Complete proteome {ECO:0000313|Proteomes:UP000050514};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050514}.
FT   DOMAIN      142    269       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      350    419       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     150    157       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   443 AA;  49666 MW;  07A5F4C9478A8ADA CRC64;
     MNAQQAWQAA LGQLQMEMPK ASFDTWVRNA ELIRVENNKA RIGVQNAYAR DWLESRLAGT
     FARLLTGYLD SPVEVEFVVW HRDAEHESAA PSEIVSHSNG NGNGNGNRCL IDRYRFDNFV
     VGASNRMAHA ACVAVAEKPA HAYNPLFLYG GVGLGKTHLL HAIGNAATEK GLQVLYVSSE
     DFTNELINAI RTQNTLAFRE RYRSMDVLLI DDIQFIAGKE STQEEFFHTF NTLHNQEKQI
     VLSSDRPPKA MVTLEERLRS RFEWGLTVDI QPPDLETRIA ILRSKAMRAG REVPMDILTL
     IARQIQSNIR ELEGALTRIL AYSDLSNQPI TAKLVEIALA DLLPQQSTVE PGAIITAVGR
     VFGVSREKLV GRDRSREVAL PRQVAMYLMR EIGGLSLPQI GEALGGRDHT TVLYACEKIA
     DQIERDDRLR RQVLNVREQV LGR
//
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