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Database: UniProt
Entry: A0A176U5N2_9FIRM
LinkDB: A0A176U5N2_9FIRM
Original site: A0A176U5N2_9FIRM 
ID   A0A176U5N2_9FIRM        Unreviewed;       459 AA.
AC   A0A176U5N2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   25-OCT-2017, entry version 12.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=HMPREF2738_01924 {ECO:0000313|EMBL:OAD88063.1};
OS   Clostridiales bacterium KLE1615.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales.
OX   NCBI_TaxID=1715004 {ECO:0000313|EMBL:OAD88063.1, ECO:0000313|Proteomes:UP000077212};
RN   [1] {ECO:0000313|EMBL:OAD88063.1, ECO:0000313|Proteomes:UP000077212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLE1615 {ECO:0000313|EMBL:OAD88063.1,
RC   ECO:0000313|Proteomes:UP000077212};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
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:OAD88063.1}.
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DR   EMBL; LXPQ01000148; OAD88063.1; -; Genomic_DNA.
DR   RefSeq; WP_066561137.1; NZ_KV441351.1.
DR   EnsemblBacteria; OAD88063; OAD88063; HMPREF2738_01924.
DR   PATRIC; fig|1715004.3.peg.1915; -.
DR   Proteomes; UP000077212; 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   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; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000077212};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077212}.
FT   DOMAIN      152    280       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      364    433       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     160    167       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   459 AA;  52496 MW;  F003BD3766261894 CRC64;
     MIDRLKENWD AIKDTLKENY DISKVSYDTW IVPMEIHNVD NDQVYILADT KGIPNILDYI
     KKKYKQILEI VIEEKIGLHC NVIFVTSEDL EKRPNLTAEA SNIVTPELNS YYAAVMNANL
     NPRYTFDTFV VGSNNRFAHA ASLAVAESPG TLYNPLFIYG GAGLGKTHLM QSIAHYILRN
     DPSVRVLYVT SETFTNDLID SLKGKKNAEF KEKYRSIDVL MIDDIQFLIG KESTQEEFFH
     TFNYLYETGK QVIITSDKPP KDFTNLEERL RSRFSVGLPV DVSAPDYETR VAILHKKEET
     ENTKISDDII NYIAENINTN IRELEGALNR ITAFKRLSNK EITLSMAEDV LRDIINNHKE
     VTITVPLIVE VIASHFGFEA DELLSQKRNK DIAYSRQIAM YLCRQMTDLS LQQIGKELGN
     RDHTTVRHGI EKITEDLKNS QFLQDTIDVL QKKINPALG
//
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