GenomeNet

Database: UniProt
Entry: A0A1Y4G8Z8_9ACTN
LinkDB: A0A1Y4G8Z8_9ACTN
Original site: A0A1Y4G8Z8_9ACTN 
ID   A0A1Y4G8Z8_9ACTN        Unreviewed;       514 AA.
AC   A0A1Y4G8Z8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   16-JAN-2019, entry version 12.
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=B5F40_00165 {ECO:0000313|EMBL:OUO92364.1};
OS   Gordonibacter sp. An230.
OC   Bacteria; Actinobacteria; Coriobacteriia; Eggerthellales;
OC   Eggerthellaceae; Gordonibacter.
OX   NCBI_TaxID=1965592 {ECO:0000313|EMBL:OUO92364.1};
RN   [1] {ECO:0000313|EMBL:OUO92364.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An230 {ECO:0000313|EMBL:OUO92364.1};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T.,
RA   Cizek A., Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-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}.
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:OUO92364.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; NFJP01000001; OUO92364.1; -; Genomic_DNA.
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   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      198    347       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      422    490       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     206    213       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      487    514       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   514 AA;  57526 MW;  96648010A81BAEFC CRC64;
     MNSESIEQSW QEVCSQIKSY NNIDPTQISA FFSRLHPQAM SEGFLMLTAD NDFIKTWIER
     HYAEFIQQAL IDLYHVPFTV VIEVDLAGAP PVPNAVQASG AHPPTLQPST AATAATATQT
     GPHTTPAASK TQATAQDPSK EDDGAVALPD PANPLPSTAD MADAPTSTLT FENFVIGDSN
     RMAYSMAVAV AEMPGKAHLN PLFIYGKSGL GKTHLMRAIQ NYVNETMPHL SVIYVDSAEL
     LSDYMEASAA HDKEKSSYKN FKTRYEEADV LLIDDVQYLQ GKKQTLDIVF QIFNKLTSQG
     RQVVLSADRA PKNIDIDERY KSRFNSGGTF DIQPPEIETK LGIVKSFVEE YRESEGSNDF
     DIPADIQMYI AESSSSNIRE LKSAVTKVIY QMTFFNQPML SLDDVRSLLE NHFSGGSSKR
     LTIADIQKEV EAFYKVSHAD LIGNKRTRNI TYARQIAMYL CRQMLDLPFN DIGKKFNRDH
     STVMYSVTNI ENKIKENREL SEELETLRQI IHEI
//
DBGET integrated database retrieval system