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Database: UniProt
Entry: L8J9Q5_9GAMM
LinkDB: L8J9Q5_9GAMM
Original site: L8J9Q5_9GAMM 
ID   L8J9Q5_9GAMM            Unreviewed;       470 AA.
AC   L8J9Q5;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   25-OCT-2017, entry version 34.
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=C942_02912 {ECO:0000313|EMBL:ELR64182.1};
OS   Photobacterium marinum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=1056511 {ECO:0000313|EMBL:ELR64182.1, ECO:0000313|Proteomes:UP000011134};
RN   [1] {ECO:0000313|EMBL:ELR64182.1, ECO:0000313|Proteomes:UP000011134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK15 {ECO:0000313|EMBL:ELR64182.1,
RC   ECO:0000313|Proteomes:UP000011134};
RA   Khatri I., Vaidya B., Srinivas T.N.R., Subramanian S., Pinnaka A.;
RT   "Genome Assembly of Photobacterium sp. AK15.";
RL   Submitted (DEC-2012) 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:ELR64182.1}.
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DR   EMBL; AMZO01000031; ELR64182.1; -; Genomic_DNA.
DR   RefSeq; WP_007468691.1; NZ_AMZO01000031.1.
DR   EnsemblBacteria; ELR64182; ELR64182; C942_02912.
DR   PATRIC; fig|1056511.3.peg.3836; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000011134; 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:UP000011134};
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:UP000011134}.
FT   DOMAIN      167    369       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      378    447       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     175    182       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   470 AA;  53239 MW;  34713E8CE50FB66E CRC64;
     MSSSLWLQCL QRLQEELPAT EFSMWVRPLQ AELNDNTLTL FAPNRFVLDW VRDKYLNNIN
     RLLNEFCGND VPILRFEVGS RPVTAPPPQP VAAAPVLGSP SPAPVRDEIP PPSRNWEPAP
     SPVQPESQGG YRSNVNPKHN FNNFVEGKSN QLGLAACRQV ADNPGAAYNP LFLYGGTGLG
     KTHLLHAVGN AIADRKPNAK VVYMHSERFV QDMVKALQNN AIEEFKRYYR SVDALLIDDI
     QFFANKERSQ EEFFHTFNAL LEGNQQIILT SDRYPREING VEDRLKSRFG WGLTVAIEPP
     ELETRVAILM KKAEDHNIRL ADEVAFFIAK RLRSNVRELE GALNRVIANA NFTGRAITID
     FVREALRDLL ALQEKLVTID NIQKTVAEYY KIKMADMLSK RRSRSVARPR QMAMALAKEL
     TNHSLPEIGD AFGGRDHTTV LHACRKIEQL REESHDIKED YSNLIRTLSS
//
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