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Database: UniProt
Entry: A0A0F0CMM5_9BACT
LinkDB: A0A0F0CMM5_9BACT
Original site: A0A0F0CMM5_9BACT 
ID   A0A0F0CMM5_9BACT        Unreviewed;       473 AA.
AC   A0A0F0CMM5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   05-JUL-2017, entry version 17.
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=OMAG_001626 {ECO:0000313|EMBL:KJJ84522.1};
OS   Candidatus Omnitrophus magneticus.
OC   Bacteria; Candidatus Omnitrophica; Candidatus Omnitrophus.
OX   NCBI_TaxID=1609969 {ECO:0000313|EMBL:KJJ84522.1, ECO:0000313|Proteomes:UP000033428};
RN   [1] {ECO:0000313|EMBL:KJJ84522.1, ECO:0000313|Proteomes:UP000033428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKK-01 {ECO:0000313|EMBL:KJJ84522.1};
RA   Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT   "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT   conserved set of magnetosome genes.";
RL   Submitted (FEB-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: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:KJJ84522.1}.
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DR   EMBL; JYNY01000341; KJJ84522.1; -; Genomic_DNA.
DR   EnsemblBacteria; KJJ84522; KJJ84522; OMAG_001626.
DR   PATRIC; fig|1609969.3.peg.1749; -.
DR   Proteomes; UP000033428; 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:UP000033428};
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:UP000033428}.
FT   DOMAIN      165    293       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      375    444       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     173    180       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   473 AA;  53217 MW;  ED85C678C2A29EBA CRC64;
     MDNLWEKTLS LLKKETADHV FSIWFEPITF ISFENSVLLI SVPNKFFENW LKEKYFSTLS
     SALLKTAGTP VSIQFQTKET TSIKQKAPLH GASQKNSSSS GAHTSPEPEI DNINTIIKNS
     RLLPENLYKN TVINSKYSFE NFVVGPGNRF AHAAALSVSE NLAKSYNPLF IHGGVGLGKT
     HLLHSISHHL LKKNSSAKII YISSEEFTNQ LIQAIKTKTT TKFRNMYRHV DILLIDDIQF
     LAGKEATQEE FFHTFNSLHD SHKQIVISSD RSPKEIPTLE ERLVSRFAWG LIADVQPPEV
     ETRIAILEKK AENEDISIPK DVLVFLAEKI TTNIRELEGA LIRVVAYSKL IGTPLSLSLA
     KQTLQGMIAE EKKIRIKDII ETVTDYFDIT SDSIQAKTRA RAIAYPRQIA MYLCRNLTDH
     SFPDIGGFFG GRDHTTVLHA YEKINKAVGE NDKTKDLIQT LTIKIKGNTA VPF
//
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