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Database: UniProt
Entry: A0A133YQP3_9FIRM
LinkDB: A0A133YQP3_9FIRM
Original site: A0A133YQP3_9FIRM 
ID   A0A133YQP3_9FIRM        Unreviewed;       477 AA.
AC   A0A133YQP3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   25-OCT-2017, entry version 13.
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=HMPREF3188_00946 {ECO:0000313|EMBL:KXB45461.1};
OS   Tissierellia bacterium KA00581.
OC   Bacteria; Firmicutes; Tissierellia.
OX   NCBI_TaxID=1588751 {ECO:0000313|EMBL:KXB45461.1, ECO:0000313|Proteomes:UP000070503};
RN   [1] {ECO:0000313|EMBL:KXB45461.1, ECO:0000313|Proteomes:UP000070503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA00581 {ECO:0000313|EMBL:KXB45461.1,
RC   ECO:0000313|Proteomes:UP000070503};
RA   Oliw E.H.;
RL   Submitted (JAN-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: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:KXB45461.1}.
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DR   EMBL; LSCW01000062; KXB45461.1; -; Genomic_DNA.
DR   RefSeq; WP_068552154.1; NZ_KQ959646.1.
DR   EnsemblBacteria; KXB45461; KXB45461; HMPREF3188_00946.
DR   PATRIC; fig|1588751.3.peg.936; -.
DR   Proteomes; UP000070503; 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   Complete proteome {ECO:0000313|Proteomes:UP000070503};
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:UP000070503}.
FT   DOMAIN      169    302       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      386    454       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     177    184       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   477 AA;  54526 MW;  77ADDC5334EA677C CRC64;
     MLENEIDVKS LWLQICNILK SKLNDFRYAA WIEVLKPVCY FENTLMVLCP SEFIKTSVNT
     TFKAYIEDVI NTILSDITDK KTILLVVTST DKEYLDYMNN SGVGQVSFIC NDSKENKTTT
     KKKKLKNKIV DDDSMSFPDR YTFDNFVTGG NSEFAVAASR AVAENPGLSY NPLFIYGNPG
     LGKTHLMKAI GHEINKNFDC KILYTTSENL LTDLVNLIQK KGIDPNINSK FIAKYRSVDV
     LLIDDIQFMV GKDRTQEEFF HIFNELYSKN KQIVISSDRP ANDLKNLEER LKSRFNMGLT
     VDIQFPDFET RLAILQNKMK LESIELTNEI LEFIAMNIKT NIRDLEGALI NVLAHYKLKK
     NAPMTVDYVK TILCKKLNEI NKKEITIDLI KETVAKYFKI NISDLSSKNR SSSISYPRQV
     AMYLCRNMLD CALGNIGDAF EKDHTTIMHG VKQIDKKIKT SDSIKKDVDT LKKLIEG
//
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