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Database: UniProt
Entry: A0A0M2R6J5_9PROT
LinkDB: A0A0M2R6J5_9PROT
Original site: A0A0M2R6J5_9PROT 
ID   A0A0M2R6J5_9PROT        Unreviewed;       476 AA.
AC   A0A0M2R6J5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   25-OCT-2017, entry version 16.
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=WH95_15000 {ECO:0000313|EMBL:KKJ76064.1};
OS   Kiloniella litopenaei.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Kiloniellales;
OC   Kiloniellaceae; Kiloniella.
OX   NCBI_TaxID=1549748 {ECO:0000313|EMBL:KKJ76064.1, ECO:0000313|Proteomes:UP000034491};
RN   [1] {ECO:0000313|EMBL:KKJ76064.1, ECO:0000313|Proteomes:UP000034491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1-1 {ECO:0000313|EMBL:KKJ76064.1,
RC   ECO:0000313|Proteomes:UP000034491};
RA   Shao Z., Wang L., Li X.;
RT   "Genome sequence of Kiloniella sp. P1-1, isolated from the gut
RT   microflora of Pacific white shrimp, Penaeus vannamei.";
RL   Submitted (MAR-2015) 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:KKJ76064.1}.
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DR   EMBL; LANI01000022; KKJ76064.1; -; Genomic_DNA.
DR   RefSeq; WP_046508713.1; NZ_LANI01000022.1.
DR   EnsemblBacteria; KKJ76064; KKJ76064; WH95_15000.
DR   PATRIC; fig|1549748.8.peg.1753; -.
DR   Proteomes; UP000034491; 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:UP000034491};
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:UP000034491}.
FT   DOMAIN      173    301       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      384    453       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     181    188       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   476 AA;  54036 MW;  29ACE7FA07E39E26 CRC64;
     MAQSEVVLSF QEQWDRVLGK LRTEVGEAAY RSWLKPLSLL SGDESFIRMA VPTRFMRDWV
     ASNYQDRIQA LWLEEIGTPI DVEIVVLSPS RPVPKPALVD VKDEPEVLRA QERDVPVLPV
     ATDLPVEAVQ ESDVQQITGS LDPRFTFENF VVGKPNELAY AAAQRVADAE AVPFNPLFLY
     GGVGLGKTHL MHAIAHQIRK AHPEKKVIYL SAEKFMYQFV RALRTKDTMS FKEQFRSVDV
     LMIDDVQFIG GREATQEEFF HTFNALVDQN RQVIISADKS PSDLEGVEER MKSRLGWGLV
     ADIHPTTYEL RLGILESKAE QLDVEIPQKV IEFLAHKITS NIRELEGALN RIVAHATLVG
     RSVTLETTQE VLHDLLRAND RRVTIEEIQK KVAEHFNVRV SDMHSARRAR AVARPRQIAM
     YLSKQLTSRS LPEIGRKFGG RDHTTVMHAV KKVEELKATD LEFAEDIELL SRMLEN
//
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