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Database: UniProt
Entry: A0A0P1IHD3_9RHOB
LinkDB: A0A0P1IHD3_9RHOB
Original site: A0A0P1IHD3_9RHOB 
ID   A0A0P1IHD3_9RHOB        Unreviewed;       532 AA.
AC   A0A0P1IHD3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-SEP-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   ECO:0000313|EMBL:CUK13345.1};
GN   ORFNames=PH7735_03794 {ECO:0000313|EMBL:CUK13345.1};
OS   Phaeobacter sp. CECT 7735.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Phaeobacter.
OX   NCBI_TaxID=1715693 {ECO:0000313|EMBL:CUK13345.1, ECO:0000313|Proteomes:UP000051870};
RN   [1] {ECO:0000313|EMBL:CUK13345.1, ECO:0000313|Proteomes:UP000051870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7735 {ECO:0000313|EMBL:CUK13345.1,
RC   ECO:0000313|Proteomes:UP000051870};
RG   Swine Surveillance;
RL   Submitted (SEP-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:SAAS00756131}.
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; CYTW01000006; CUK13345.1; -; Genomic_DNA.
DR   EnsemblBacteria; CUK13345; CUK13345; PH7735_03794.
DR   Proteomes; UP000051870; 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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051870};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051870}.
FT   DOMAIN      224    354       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      440    509       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     232    239       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   532 AA;  59820 MW;  900F3CE0ABDBDE59 CRC64;
     MLVFIVLLLC FLGKCILRMH GQDLLSGDSF RGGNRSLHAA EMPPQKGQAV SIRTEGRKTG
     PNGPSDERLR ARKWGQMTQE QWGALQGNLL NTVGQNNYKT WIEPLEFAEL EDGVATFHVP
     TNFIGNYVSQ NFGDLILHQL STTGESIQRV HFKVPASAAT APKARPAVSS PSMAKKAAAP
     APARDSLPGA PLDARFTFDS FVVGKPNELA NAAARRVAEG GPVTFNPLFL YGGVGLGKTH
     LMHAIAWELQ KRRPDLNVLY LSAEQFMYRF VQALRDRKMM DFKEMFRSVD VLMVDDVQFI
     AGKDSTQEEF FHTFNALVDQ NKQIIISADR APGEIKDLED RIKSRLQCGL VVDLHPTDYE
     LRLGILQSKV EQYRVQYPDL QLADGVLEFL AHRISTNVRV LEGALTRLFA FASLVGREIT
     MELTQDCLSD VLRASERKIS VEEIQRRVAE HYNIRLSDMI GPKRVRTLAR PRQIAMYLCK
     QLTSRSLPEI GRRFGGRDHT TVMHGVRRIE ELRVQDGQIA EDLELLRRSL EA
//
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