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Database: UniProt
Entry: A0A222SF34_9CHLB
LinkDB: A0A222SF34_9CHLB
Original site: A0A222SF34_9CHLB 
ID   A0A222SF34_9CHLB        Unreviewed;       493 AA.
AC   A0A222SF34;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   13-FEB-2019, entry version 11.
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=CHL67_00005 {ECO:0000313|EMBL:ASQ89535.1};
OS   Prosthecochloris sp. GSB1.
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=281093 {ECO:0000313|EMBL:ASQ89535.1, ECO:0000313|Proteomes:UP000201322};
RN   [1] {ECO:0000313|EMBL:ASQ89535.1, ECO:0000313|Proteomes:UP000201322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TY Vent \ GSB1 \ Ty-1 {ECO:0000313|Proteomes:UP000201322};
RA   Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL   Submitted (JUL-2017) 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; CP022571; ASQ89535.1; -; Genomic_DNA.
DR   KEGG; pros:CHL67_00005; -.
DR   KO; K02313; -.
DR   BioCyc; GCF_002240205:CHL67_RS00005-MONOMER; -.
DR   Proteomes; UP000201322; Chromosome.
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:UP000201322};
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:UP000201322}.
FT   DOMAIN      187    323       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      398    467       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     195    202       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      467    493       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   493 AA;  55880 MW;  4C827D2A3B955EB4 CRC64;
     MPQPSTGELV EEQPSVSSAR SGMAQKLWDS CLAVLRDKIN SQAFKTWFTP IRPIHFSDSE
     LTIEVPSQFF YEWIEENYSK QLKQALKDIL GVEGRLRYSV VMDKSQTHPV TIELPHQNIV
     KPGEEDGQDT YRGSRTSTER EYIERNRAKF ESHLNPKYIF DSLIRGDCNS LAFAASKSVA
     QNPGQNAFNP LVIYGGVGLG KTHMIQAIGN QVREQKISDN VLYVSSEKFA IDFVNAIQNG
     TIQEFSAFYR QVDVLMIDDI QFFAGKEKTQ EEIFHIFNAL HQSNKQIILS SDRPIKDIRG
     IEDRLISRFN WGLSADIQPP DYETRKAIIQ SKLELNGVIL DESVTEFIAT NVTHNVRELE
     GCIVKLLAAH SLFDQDIDLA FTKSTLKDII RIQSKQLTLE TIEKAVCSFF SITPNDLKGK
     SKKKEIAAGR QIAMFLSKEL TDSSLKTIGL HFGGRDHSTV IHGYNTIRKK VGQSNELRSQ
     LEELKKRIEI MSI
//
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