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Database: UniProt
Entry: A0A0S2HUD2_9BACT
LinkDB: A0A0S2HUD2_9BACT
Original site: A0A0S2HUD2_9BACT 
ID   A0A0S2HUD2_9BACT        Unreviewed;       474 AA.
AC   A0A0S2HUD2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   05-JUL-2017, entry version 13.
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_1 {ECO:0000313|EMBL:ALO13683.1};
GN   Synonyms=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=L21SP5_00001 {ECO:0000313|EMBL:ALO13683.1};
OS   Salinivirga cyanobacteriivorans.
OC   Bacteria; Bacteroidetes; Bacteroidia; Marinilabiliales;
OC   Salinivirgaceae; Salinivirga.
OX   NCBI_TaxID=1307839 {ECO:0000313|EMBL:ALO13683.1, ECO:0000313|Proteomes:UP000064893};
RN   [1] {ECO:0000313|EMBL:ALO13683.1, ECO:0000313|Proteomes:UP000064893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L21-Spi-D4 {ECO:0000313|EMBL:ALO13683.1,
RC   ECO:0000313|Proteomes:UP000064893};
RA   Spring S., Bunk B., Sproer C., Klenk H.-P.;
RT   "Description and complete genome sequence of a novel strain
RT   predominating in hypersaline microbial mats and representing a new
RT   family of the Bacteriodetes phylum.";
RL   Submitted (NOV-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:SAAS00756131}.
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; CP013118; ALO13683.1; -; Genomic_DNA.
DR   RefSeq; WP_057951324.1; NZ_CP013118.1.
DR   EnsemblBacteria; ALO13683; ALO13683; L21SP5_00001.
DR   KEGG; blq:L21SP5_00001; -.
DR   PATRIC; fig|1307839.3.peg.1; -.
DR   KO; K02313; -.
DR   Proteomes; UP000064893; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000064893};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000064893}.
FT   DOMAIN      171    301       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      382    451       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     179    186       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   474 AA;  54277 MW;  CC3B6517E556B891 CRC64;
     MDHKEAWDHC LSIIRDNIPE RSFQTWFSPI RPIKLSDKVL TIEVPTSFFY EYLEEHFIDI
     LRKTLFKVIG ADAKLEYSII VHNNTHNSKP YAVKIPTQNK SDLTNRPVSM PMGSNSTNNI
     KNPFVIPGIQ KLNIDPQLNS DYNFQNFIEG ECNRLARSAG FAIAQNPGKT AFNPLFIYGA
     SGLGKTHLAH AIGIQVKERF PEKTVLYVEA NKFERQYADA TRSNERNDFV HFYQMIDVLI
     IDDVQHLAAK QKTQDVFFHI FNHLHQSGKQ LILTSDKPPV ELEGLEQRLL SRFKWGLSAD
     LQVPDFETRK TILQKMAYKD GIELQDEIID YIANHINTNV RELEGALVSL MAQSTLNRKE
     ITIDLAKDLI DKLVSNTRKE ITLDVIQQTV CDYFSMPVDQ LKSKTRKREI VQARQIAMYF
     AKSKTKSSLS TIGARIGGKD HATVLHACKT VKNLLDTDKR FKSFVTDIDK MLEN
//
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