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Database: UniProt
Entry: A0A263HDG6_9PAST
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Original site: A0A263HDG6_9PAST 
ID   A0A263HDG6_9PAST        Unreviewed;       465 AA.
AC   A0A263HDG6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   16-JAN-2019, entry version 9.
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   ECO:0000313|EMBL:OZN25092.1};
GN   Synonyms=dnaA_1 {ECO:0000313|EMBL:SUU33757.1};
GN   ORFNames=CFY87_05110 {ECO:0000313|EMBL:OZN25092.1}, NCTC10851_00001
GN   {ECO:0000313|EMBL:SUU33757.1};
OS   Actinobacillus seminis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=722 {ECO:0000313|EMBL:OZN25092.1, ECO:0000313|Proteomes:UP000215738};
RN   [1] {ECO:0000313|EMBL:OZN25092.1, ECO:0000313|Proteomes:UP000215738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15768 {ECO:0000313|EMBL:OZN25092.1,
RC   ECO:0000313|Proteomes:UP000215738};
RA   Negrete-Abascal E., Vaca-Pacheco S., Montes-Garcia F., Leyto-Gil A.M.,
RA   Fragoso-Garcia E., Carvente-Garcia R., Perez-Agueros S.,
RA   Castelan-Sanchez H.G., Garcia-Molina A., Villamar T.E.,
RA   Vazquez-Cruz C.;
RT   "Virulence factors identified in Actinobacillus seminis.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SUU33757.1, ECO:0000313|Proteomes:UP000254507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10851 {ECO:0000313|EMBL:SUU33757.1,
RC   ECO:0000313|Proteomes:UP000254507};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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; NLFK01000004; OZN25092.1; -; Genomic_DNA.
DR   EMBL; UFSB01000001; SUU33757.1; -; Genomic_DNA.
DR   Proteomes; UP000215738; Unassembled WGS sequence.
DR   Proteomes; UP000254507; 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:UP000215738,
KW   ECO:0000313|Proteomes:UP000254507};
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:UP000215738}.
FT   DOMAIN      150    286       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      373    442       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     158    165       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      289    309       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   465 AA;  53181 MW;  3A07FEBCBB158C7D CRC64;
     MKPTSMSLWQ DCLLLLQDQI SATDFDTWLR PLQADISSDN TIVLYAPNIF VRSWVEAHYL
     EQITKLVQQL AQNTNLIVRI QDGIKPAAKP VQRQETVVSQ PVVSEEEEGK STYRSNLNTK
     QVFENFVEGK SNQLARAIAQ KVANNPGEQS ANPLFLYGGT GLGKTHLLHA VGNGICTNNP
     NARVIYIHAE RFMQEYVKSL KSDTMEKFKK FYRTLDALLI DDIQFFAGKD GTQEEFFHIF
     NSLFESSRQI ILTSDRYPKE IEKIEDRLKS RFGWGLTIAI EPPDLETRVA ILLKKAEEKN
     QERREKEDKE LIILPEEVAF FVGQKLRSNV RELEGSLNKL FAMAEFKGEK VISIDFVRET
     LKDMLALQDK LVTVDNIQKV VAEYYRIKVS DLKSKNRSRS IARPRQLAMA LAKELTNRSL
     PEIGKGFGDR DHTTVLHACR TIATLRKEDN NIQEDWSNLI RTLSA
//
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