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Entry: B0PBN1_9FIRM
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ID   B0PBN1_9FIRM            Unreviewed;       439 AA.
AC   B0PBN1;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   23-MAY-2018, entry version 68.
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   ECO:0000313|EMBL:EDS11006.1};
GN   ORFNames=ANACOL_02189 {ECO:0000313|EMBL:EDS11006.1};
OS   Anaerotruncus colihominis DSM 17241.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Anaerotruncus.
OX   NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS11006.1, ECO:0000313|Proteomes:UP000003803};
RN   [1] {ECO:0000313|EMBL:EDS11006.1, ECO:0000313|Proteomes:UP000003803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS11006.1,
RC   ECO:0000313|Proteomes:UP000003803};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M.,
RA   Liep D., Gordon J.;
RT   "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS11006.1, ECO:0000313|Proteomes:UP000003803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS11006.1,
RC   ECO:0000313|Proteomes:UP000003803};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H.,
RA   Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (NOV-2007) 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:SAAS00747961}.
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:EDS11006.1}.
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DR   EMBL; ABGD02000018; EDS11006.1; -; Genomic_DNA.
DR   RefSeq; WP_006873105.1; NZ_DS544171.1.
DR   ProteinModelPortal; B0PBN1; -.
DR   STRING; 445972.ANACOL_02189; -.
DR   EnsemblBacteria; EDS11006; EDS11006; ANACOL_02189.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000003803; 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:SAAS00747950};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003803};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00747973};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00748008};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003803}.
FT   DOMAIN      134    262       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      346    415       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     142    149       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      296    316       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   439 AA;  49663 MW;  0D3B47DDE9BA5C91 CRC64;
     MDSFAELFAL VLDLCKNQIS DVAFNLWLKD IIPLRLEGSA AFLQVNSEFK MNIIREKYTS
     ILKSAFETTL GFPVDVIITC ETPQPAEKPA GPPPSDAAAV NGEYDYTFDT FIVGSSNKFA
     HAASLAVAAN PANAYNPLFI YGGSGLGKTH LLYAICAEIR KNRPNYNIIY VKGDEFANDI
     ITAIRDQRTA EFRERYRKAD VLLVDDIQFI GGKESTQEEF FHTFNTLYES NKQIVLASDR
     PPKEIKTLED RLRTRFEWGL LADIQIPDFE TRIAIIRRKA QLLDIQMPDD VAEYIANRLK
     TNIRQLEGTV KKLKAYKLLQ GTNPSIMIAQ NAIRDILNDN QPVPVTVERI ISEVGRTYGI
     SPQDIRSNKR SAQISAARQI SIYIVREITQ MSMSTIGDEF GGRDHSTIVY AIQQVEKNMN
     NDLRYKETIE DIIKNIRDS
//
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