ID A0A0B6X2J9_9BACT Unreviewed; 493 AA.
AC A0A0B6X2J9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 28-MAR-2018, entry version 26.
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=PYK22_02822 {ECO:0000313|EMBL:CDM66784.1};
OS Pyrinomonas methylaliphatogenes.
OC Bacteria; Acidobacteria; Blastocatellia; Blastocatellales;
OC Pyrinomonadaceae; Pyrinomonas.
OX NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM66784.1, ECO:0000313|Proteomes:UP000031518};
RN [1] {ECO:0000313|EMBL:CDM66784.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM66784.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Stott M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDM66784.1, ECO:0000313|Proteomes:UP000031518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K22 {ECO:0000313|EMBL:CDM66784.1,
RC ECO:0000313|Proteomes:UP000031518};
RA Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA Stott M.B.;
RT "Complete genome sequence of Pyrinomonas methylaliphatogenes type
RT strain K22T.";
RL Submitted (JAN-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:SAAS00747961}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC ECO:0000256|SAAS:SAAS00555179}.
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DR EMBL; CBXV010000008; CDM66784.1; -; Genomic_DNA.
DR RefSeq; WP_041978237.1; NZ_CBXV010000008.1.
DR EnsemblBacteria; CDM66784; CDM66784; PYK22_02822.
DR Proteomes; UP000031518; 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 Complete proteome {ECO:0000313|Proteomes:UP000031518};
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:RU004227, 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:UP000031518}.
FT DOMAIN 189 317 AAA. {ECO:0000259|SMART:SM00382}.
FT DOMAIN 401 470 Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT NP_BIND 197 204 ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ SEQUENCE 493 AA; 56406 MW; 88C25F03231D669A CRC64;
MRTSVEDRIW NDLLQAIERR LNRQSFETWF RPIRFEGCDE ARHVLRLCAP NQVVKDWVSS
NYSDILRASL EELNLASYHV DWKVEDEEQQ TERIMNEEFI SYNDDSLDLS SDKDLSGQPL
PKGKGTSFLP LLEAAEAEGL MPGSTTFVDI EPMELSLNPK YTFQTFVVGS CNQFAHAAAL
AVAEAPGKTY NPLYIYGGVG LGKTHLMHAI GHFIRERNRH LRLSYISAER FMNELINAIR
YDKVQAFREK YRFIDVLLMD DVQFMAGKER TQEEFFHTFN ALYDAQKQIV ITSDCPPRGI
PMIEERLHSR FEWGLIADIE PPDLETKVAI LKRKADLDGV ELPDDVAFFI ASKVKSNIRE
LEGSLVRLVA ISSLRGLPIS IMLAQDAIRN IAEDDRPAGI TIEQIQRAVA QHYKLRVEDL
KSKNNSRQIA VPRQIAMYLC KKLTKHSFPE IGREFGGKHH TTVIHSVEKI ESLVEKDPNF
HRVVSDIIDS ICK
//