ID A0A4Q1SJB2_9BACT Unreviewed; 476 AA.
AC A0A4Q1SJB2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 08-NOV-2023, entry version 15.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN ECO:0000313|EMBL:RXS97716.1};
GN ORFNames=ESZ00_07550 {ECO:0000313|EMBL:RXS97716.1};
OS Silvibacterium dinghuense.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Silvibacterium.
OX NCBI_TaxID=1560006 {ECO:0000313|EMBL:RXS97716.1, ECO:0000313|Proteomes:UP000290253};
RN [1] {ECO:0000313|EMBL:RXS97716.1, ECO:0000313|Proteomes:UP000290253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOF10 {ECO:0000313|EMBL:RXS97716.1,
RC ECO:0000313|Proteomes:UP000290253};
RX PubMed=26475169; DOI=.1099/ijsem.0.000676;
RA Jiang Y.W., Wang J., Chen M.H., Lv Y.Y., Qiu L.H.;
RT "Acidipila dinghuensis sp. nov., an acidobacterium isolated from forest
RT soil.";
RL Int. J. Syst. Evol. Microbiol. 66:76-83(2016).
CC -!- FUNCTION: Plays an important role in the initiation and regulation of
CC chromosomal replication. Binds to the origin of replication; it binds
CC specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-
CC TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
CC {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00377}.
CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|ARBA:ARBA00006583,
CC ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU004227}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXS97716.1}.
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DR EMBL; SDMK01000001; RXS97716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q1SJB2; -.
DR OrthoDB; 9807019at2; -.
DR Proteomes; UP000290253; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; cd00009; AAA; 1.
DR CDD; cd06571; Bac_DnaA_C; 1.
DR Gene3D; 1.10.1750.10; -; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.300.180; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR038454; DnaA_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010921; Trp_repressor/repl_initiator.
DR NCBIfam; TIGR00362; DnaA; 1.
DR PANTHER; PTHR30050; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1.
DR PANTHER; PTHR30050:SF2; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48295; TrpR-like; 1.
DR PROSITE; PS01008; DNAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00377};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00377};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00377};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00377};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00377}; Reference proteome {ECO:0000313|Proteomes:UP000290253}.
FT DOMAIN 173..301
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 384..453
FT /note="Chromosomal replication initiator DnaA C-terminal"
FT /evidence="ECO:0000259|SMART:SM00760"
FT REGION 87..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 181..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ SEQUENCE 476 AA; 53814 MW; DDAB6DC9C189A132 CRC64;
MSFVATPATV LNPWVRILGA LEKKINRQSF DTWLKPTRFS HAKERLLYVR IPTPEFQHVG
DHYGDLIQEA IDALQLEFDD VKFVTPEDDP TLAQPREDGG FPPVPTHAPN APASNRNGYA
RNNAPAPPQQ GRFDWSSAAQ LNPRYTFDAF VIGAGNQFAR AAAEAVAERP SKAYNPLFLY
GGTGMGKTHL MQAVGHEVKQ RIPNASICYV SVEKFTNEMI NSLRYDKMTS FRDKFRSVDL
LLIDDIQFLS QKERTQEEFF HTFNALHENM KQIVIASDRP PKELPEIEDR LRSRFEWGLI
ADIQPPDLET KVAILQKKAE SEHVALPTDV ALFIASNVRT NVRELEGALT RLFAWSSLNG
VELTLPTAQQ CLKQFIDTQV RKITIEAIQR AVAEQFGMRV AELKQKNNSR AVVVPRQIAM
YLAKQMTEAS LPEIGRQFGG KHHTTVMHSI AKIDEQRRAD KNLNSTLNKL NETLNN
//
