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Database: UniProt
Entry: A0A077MEE4_9MICO
LinkDB: A0A077MEE4_9MICO
Original site: A0A077MEE4_9MICO 
ID   A0A077MEE4_9MICO        Unreviewed;       488 AA.
AC   A0A077MEE4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 26.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:CCI53283.1};
GN   ORFNames=BN13_330041 {ECO:0000313|EMBL:CCI53283.1};
OS   Tetrasphaera jenkinsii Ben 74.
OC   Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae;
OC   Tetrasphaera.
OX   NCBI_TaxID=1193518 {ECO:0000313|EMBL:CCI53283.1, ECO:0000313|Proteomes:UP000035720};
RN   [1] {ECO:0000313|EMBL:CCI53283.1, ECO:0000313|Proteomes:UP000035720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ben 74 {ECO:0000313|EMBL:CCI53283.1,
RC   ECO:0000313|Proteomes:UP000035720};
RX   PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA   Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA   Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA   Nielsen K.L., Nielsen P.H.;
RT   "A metabolic model for members of the genus Tetrasphaera involved in
RT   enhanced biological phosphorus removal.";
RL   ISME J. 7:543-554(2013).
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:SAAS00735475}.
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:CCI53283.1}.
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DR   EMBL; CAJC01000143; CCI53283.1; -; Genomic_DNA.
DR   RefSeq; WP_048545503.1; NZ_HF571038.1.
DR   EnsemblBacteria; CCI53283; CCI53283; BN13_330041.
DR   Proteomes; UP000035720; 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; 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   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:UP000035720};
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:UP000035720}.
FT   DOMAIN      172    308       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      384    453       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     180    187       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   488 AA;  54317 MW;  70A8C492225F1EC3 CRC64;
     MTDGARERAR IWSEVLTRLE SDGVSAQQRA FLTGSELKGL LDDTALIAVP TDYAKTMLET
     RIRVPVEQAL AHALEQPTKV AVTVDPSLDV EEEPASEPIA PEPRTGPVTL FDALDDEPAP
     RNAASPRHTQ QPEKVELTRL NPKYLFDTFV IGASNRFAHA AAVAVAEAPA KAYNPLFIYG
     ESGLGKTHLL HAIGHYARSL YPHVKVRYVN SEEFTNDFIN SIRDDRAANF QSRYREVDVL
     LIDDIQFLSG KVQTQEEFFH TFNTLHNANK QVVITSDVHP KQLSGFEQRM VSRFEWGLLT
     DVQPPDLETR MAILGKKALQ ERLTVPADVT EYIASRISTN IRELEGALIR VTAFASLNRQ
     PVDLPLTQIV LRDLMPVESA NQTSAATIIA QTAAYFGLTI EDLQGASRSR VLVTARQIAM
     YLCRELTDLS LPKIGQQFGG RDHTTVMHAD KKIRQLMAER RAIYNQVTEL TNRIKQQGSA
     RGAAPVVD
//
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