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Database: UniProt
Entry: A0A1I5TX93_9FIRM
LinkDB: A0A1I5TX93_9FIRM
Original site: A0A1I5TX93_9FIRM 
ID   A0A1I5TX93_9FIRM        Unreviewed;       465 AA.
AC   A0A1I5TX93;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   13-FEB-2019, entry version 15.
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=SAMN04487928_11085 {ECO:0000313|EMBL:SFP87700.1};
OS   Butyrivibrio proteoclasticus.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=43305 {ECO:0000313|EMBL:SFP87700.1, ECO:0000313|Proteomes:UP000182624};
RN   [1] {ECO:0000313|EMBL:SFP87700.1, ECO:0000313|Proteomes:UP000182624}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P18 {ECO:0000313|EMBL:SFP87700.1,
RC   ECO:0000313|Proteomes:UP000182624};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOXO01000010; SFP87700.1; -; Genomic_DNA.
DR   RefSeq; WP_074887021.1; NZ_FOXO01000010.1.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; GCF_900115735:G1FNO-2410-MONOMER; -.
DR   Proteomes; UP000182624; 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:UP000182624};
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:UP000182624}.
FT   DOMAIN      156    287       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      371    440       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     164    171       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED       96    116       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   465 AA;  53609 MW;  4808D75BBF0F5754 CRC64;
     MQSSKEITKK LRDNWESIKH TIKIESGITE ISYRTWIDPL TVYSVQDNNV KILIPSDNSM
     ALQYIINHYM DFIRVTISEF LEIMIDVTFI LNKDIINNEE TQNVNDENNA RTYENNANYE
     HSNLNPKYRF DTFVVGSNNK FAHSASLAVA ESPGISYNPL FLYGGPGLGK THLMHSIGHF
     IMEHDHRAKV LYVTSEQFTN EVIESIRSGK TESMSKLREK YRTVDVLMVD DVQFIIGKES
     TQEEFFHTFN ELHQAGKQII LSSDKPPKEM ETLEERFRSR FEMGLIADIQ SPDYETRMAI
     LRKNSENYGK NIDDQVIDYI ATNIKSNIRE LEGAYNKIIA YSRLNNVDVT LENAMEALKD
     IIYPDKSKVI TPQLIIDTVC EQYGTKKEDI LSKKRNSDIV LPRQIIMYLC RIHTDSSLEE
     IGKLLGKKDH TTVMNGINKI KKKIAVDDEL NKNIDIIMKK INPSL
//
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