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Database: UniProt
Entry: A0A0S7ZBJ2_9BACT
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ID   A0A0S7ZBJ2_9BACT        Unreviewed;       469 AA.
AC   A0A0S7ZBJ2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   25-OCT-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 {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=AMS19_00485 {ECO:0000313|EMBL:KPJ84494.1};
OS   Gemmatimonas sp. SG8_23.
OC   Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae;
OC   Gemmatimonas.
OX   NCBI_TaxID=1703356 {ECO:0000313|EMBL:KPJ84494.1, ECO:0000313|Proteomes:UP000051174};
RN   [1] {ECO:0000313|EMBL:KPJ84494.1, ECO:0000313|Proteomes:UP000051174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_23 {ECO:0000313|EMBL:KPJ84494.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur
RT   cycling among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPJ84494.1}.
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DR   EMBL; LJNO01000003; KPJ84494.1; -; Genomic_DNA.
DR   PATRIC; fig|1703356.3.peg.3009; -.
DR   Proteomes; UP000051174; 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:UP000051174};
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:UP000051174}.
FT   DOMAIN      161    291       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      375    444       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     169    176       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   469 AA;  52751 MW;  F5A34C12980CF060 CRC64;
     MELTAPEVWA RIQDAVRDAV PDHAFSSWIE GVRAVALTDE ELLLEAGNRF KAEWLEDKYG
     DLLEARGAEV LGRPLRIAVR GATSPDTFTP PVVRLESPAS SESDTTPRSA PRTPASAQSR
     LLTARNPGLN ERYTFERFVV GPNNQLATAA ASAAADQPGR LYNPLVFYGG VGLGKTHLMH
     AIGHRVLQSN PDARVAYVSA EQFMNEMITA IQRGTTAQFR ARYREMDLLL LDDVQFLKNK
     ESTQDEFFHT FNALYDSHRQ IVLTGDRPPR ELEGVEERLV SRFDWGLTVD LRPPDLETRI
     AILRSKSEEE GLVLDADVIE CIAHSCTSSV RELEGAVIKL LAVSSVWNQE ITPDFARRVL
     ALRRREREPI KPVASPERIQ EGIAAAWRVR PEALSAKTRT RTVTEARHVA MYAMRKMLEM
     PLSEIGACFG GRDHSTVLYS IRKVERRIEL DPAFRDRVRD VMQEIRELS
//
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