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Database: UniProt
Entry: A0A1Y4CIA1_9FIRM
LinkDB: A0A1Y4CIA1_9FIRM
Original site: A0A1Y4CIA1_9FIRM 
ID   A0A1Y4CIA1_9FIRM        Unreviewed;       488 AA.
AC   A0A1Y4CIA1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   16-JAN-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=B5F80_05195 {ECO:0000313|EMBL:OUO46734.1};
OS   Megasphaera sp. An286.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1965622 {ECO:0000313|EMBL:OUO46734.1, ECO:0000313|Proteomes:UP000195529};
RN   [1] {ECO:0000313|EMBL:OUO46734.1, ECO:0000313|Proteomes:UP000195529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An286 {ECO:0000313|EMBL:OUO46734.1,
RC   ECO:0000313|Proteomes:UP000195529};
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:OUO46734.1}.
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DR   EMBL; NFIY01000008; OUO46734.1; -; Genomic_DNA.
DR   Proteomes; UP000195529; 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:UP000195529};
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:UP000195529}.
FT   DOMAIN      178    308       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      393    462       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     186    193       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      462    482       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   488 AA;  55365 MW;  7EC35DEBB2937248 CRC64;
     MDLATLWAGM LEQLKKVLPK PIYETWFVSS LIPTSYENDV LVLAAAQKFV CNFVNKNYAD
     QLNEAAEAVT GRPTTVKLED MNAPAAEPAK PAETDDLYKD TLFSDEDLPK APPKKKAEPE
     PKAVMVKEAN ESISPPPEEP TTEDNLIPNY TFDNFIVGNS NRIAYSIAAS VAEAPAKKYN
     PLYIYGGSGL GKTHLMHAIG HQILKNFPHM RLRCITSEDF VNDFIQAIQD KNTENFRQQY
     RNIDVLLVDD IQFLGQGDKD SSKEEFFHTF NKLYQGQKQM VFTSDRPPLD IKSLEDRLRS
     RFQSGTVTGI EPPDLETRTA ILRTWAQKEK INIDKDAINY IAANVSDNIR DLYGAYNNVL
     SMASIEKNDV TLSLTQRALK YLVAEKEEKK YITIDEITSS VCRFYSVNYN ELMGKKRTKN
     IALARQVAMY LCRELTGNTY PHIGTAFSGR DHTTVMHACE KITKMMNDSD TFKEMIERLK
     EKILDVDK
//
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