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Database: UniProt
Entry: A0A099F3F2_9RHOB
LinkDB: A0A099F3F2_9RHOB
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ID   A0A099F3F2_9RHOB        Unreviewed;       447 AA.
AC   A0A099F3F2;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   16-JAN-2019, entry version 32.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=IT41_08845 {ECO:0000313|EMBL:KGJ04761.1}, SAMN04487972_10852
GN   {ECO:0000313|EMBL:SFA51069.1};
OS   Paracoccus halophilus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=376733 {ECO:0000313|EMBL:KGJ04761.1, ECO:0000313|Proteomes:UP000029846};
RN   [1] {ECO:0000313|EMBL:KGJ04761.1, ECO:0000313|Proteomes:UP000029846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ04761.1,
RC   ECO:0000313|Proteomes:UP000029846};
RA   McGinnis J.M., Wolfgang W.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGJ04761.1, ECO:0000313|Proteomes:UP000029846}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14014 {ECO:0000313|EMBL:KGJ04761.1,
RC   ECO:0000313|Proteomes:UP000029846};
RA   Mingle L.A., Cole J.A., Lapierre P., Musser K.A.;
RT   "Paracoccus sanguinis sp. nov., isolated from clinical specimens of
RT   New York State patients.";
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SFA51069.1, ECO:0000313|Proteomes:UP000182312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6117 {ECO:0000313|EMBL:SFA51069.1,
RC   ECO:0000313|Proteomes:UP000182312};
RA   de Groot N.N.;
RL   Submitted (OCT-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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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; JRKN01000009; KGJ04761.1; -; Genomic_DNA.
DR   EMBL; FOJO01000008; SFA51069.1; -; Genomic_DNA.
DR   RefSeq; WP_036740287.1; NZ_JRKN01000009.1.
DR   EnsemblBacteria; KGJ04761; KGJ04761; IT41_08845.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000029846; Unassembled WGS sequence.
DR   Proteomes; UP000182312; 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:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029846,
KW   ECO:0000313|Proteomes:UP000182312};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029846}.
FT   DOMAIN      139    272       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      355    424       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     147    154       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   447 AA;  50260 MW;  BD94D61DBFA59D49 CRC64;
     MDKLWGQARE ELQKIIGADS FATWIEPLRL TGVDDGTATI ASPTRFLSDW VSRHYSDDIV
     KVLGRVGSPV HRVTFETRAQ TARQAAAPAR RAPAPRPAAG EELTAPLDQR FTFDNFVVGK
     PNELAHAAAL RVAAGGPVTF NPLFLYGGVG LGKTHLMHAI AREIRANQPE ARVLYLSAEQ
     FMYRFVQALR ERTVMDFKEL FRTVSVLMVD DLQFIGGKDS TQEEFFHTFN TLVDQGKQIV
     ISADRAPGEI KDMEERIKSR LQCGLIVDLH PTDYELRLGI LQSKTDAFRT QYPGLQMAPG
     VLEFLAHRIT SNVRVLEGAL QRLFAFASLM GREITLDMTQ ECLADILRAN DRKVSIEEIQ
     RKVAEHYNIR LADMIGPKRV RTVARPRQIA MYLAKQMTSR SLPEIGRRFG GRDHTTIMHG
     VRKIEELRGA DSGLAEDIDL LRRLLEA
//
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