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Database: UniProt
Entry: A0A1X4P2H5_9RHOB
LinkDB: A0A1X4P2H5_9RHOB
Original site: A0A1X4P2H5_9RHOB 
ID   A0A1X4P2H5_9RHOB        Unreviewed;       461 AA.
AC   A0A1X4P2H5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   13-FEB-2019, entry version 13.
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=MCRY_00030 {ECO:0000313|EMBL:OSQ65759.1};
OS   Marivita cryptomonadis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Marivita.
OX   NCBI_TaxID=505252 {ECO:0000313|EMBL:OSQ65759.1, ECO:0000313|Proteomes:UP000193019};
RN   [1] {ECO:0000313|EMBL:OSQ65759.1, ECO:0000313|Proteomes:UP000193019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL-SK44 {ECO:0000313|EMBL:OSQ65759.1,
RC   ECO:0000313|Proteomes:UP000193019};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Marivita cryptomonadis JCM 15447.";
RL   Submitted (MAR-2014) 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}.
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:OSQ65759.1}.
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DR   EMBL; JFKD01000001; OSQ65759.1; -; Genomic_DNA.
DR   BioCyc; GCF_002115725:MCRY_RS00030-MONOMER; -.
DR   Proteomes; UP000193019; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000193019};
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}.
FT   DOMAIN      153    283       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      369    438       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     161    168       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      438    458       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   461 AA;  52309 MW;  3499130A3DC4628A CRC64;
     MTQDQWGSIR NELHQTMGAN SFQSWIEPLI YVGTDGGIAR FNVPTNFLGN YVSQNYGDML
     LSKITRMNPS VRRIVFDTVT VSQDAPAQRK EAADATGAPL AVPQVHTKSS AKPDSLNGSP
     LDKRFTFDTF VVGKPNELAH AAARRVAEGG PVTFNPLFLY GGVGLGKTHL MHAIAWELRT
     RHPHLNVLNL SAEQFMYRFV QALRDRKMMD FKELFRSVDV LMVDDVQFIA GKDSTQEEFF
     HTFNALVDQH KQIIISADRA PDEIKDLENR IRSRLQSGLV VDLHPTDYEL RLGILQSKSE
     MYSRMYPGLE VERGILEFLA ARIVSNVRIL EGALTRLFAF ASLVGKPISM DLTQECLTDI
     LRVSERKVSI EEIQRKVADH YLIRHSDLVG PKRVRTFARP RQIAMYLCKQ LTTRSLPEIG
     RHFGGRDHTT VMHGVRRIEE LRKQDAQIAE DVELLRRSLE A
//
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