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Database: UniProt
Entry: A0A0V8T960_9CELL
LinkDB: A0A0V8T960_9CELL
Original site: A0A0V8T960_9CELL 
ID   A0A0V8T960_9CELL        Unreviewed;       523 AA.
AC   A0A0V8T960;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|ARBA:ARBA00018893, ECO:0000256|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=ATM99_09990 {ECO:0000313|EMBL:KSW29095.1};
OS   Cellulomonas sp. B6.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1295626 {ECO:0000313|EMBL:KSW29095.1, ECO:0000313|Proteomes:UP000054319};
RN   [1] {ECO:0000313|EMBL:KSW29095.1, ECO:0000313|Proteomes:UP000054319}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B6 {ECO:0000313|EMBL:KSW29095.1,
RC   ECO:0000313|Proteomes:UP000054319};
RA   Piccinni F.E., Campos E.;
RT   "Draft Genome Sequence of Cellulolytic and Xylanolytic Cellulomonas strain
RT   Isolated from Decaying Forest Soil.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KSW29095.1}.
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DR   EMBL; LNTD01000073; KSW29095.1; -; Genomic_DNA.
DR   RefSeq; WP_062102145.1; NZ_LNTD01000073.1.
DR   AlphaFoldDB; A0A0V8T960; -.
DR   STRING; 1295626.ATM99_09990; -.
DR   OrthoDB; 9807019at2; -.
DR   Proteomes; UP000054319; 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; 3.40.50.300; 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; 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   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:UP000054319}.
FT   DOMAIN          215..343
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          427..496
FT                   /note="Chromosomal replication initiator DnaA C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00760"
FT   REGION          100..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..156
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         223..230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   523 AA;  57707 MW;  D822A4CCF5FE97A8 CRC64;
     MSQDEEPARV WGHVVASLEA SPDITPRQLA FVRLAHPLGV LDGTMLLAVG NDLTKEYLET
     RVRAEVTQAL GEALGREARF AITVDPEVAG DVPPALRVVP PAPAGPSAPS ATAYEADDDG
     RPDLALVTSH PGFSPRDDAG DDANEPRAVA VPREETPDVR PALRAIDGSG PAPRRAMSEP
     ARLNPKYLFE TFVIGSSNRF AHAAAVAVAE APAKAYNPLF IYGDSGLGKT HLLHAIGHYA
     QNLYPTVRVR YVNSEEFTND FINSISEGKA GAFQRRYREV DVLLIDDIQF LQGKEQTMEE
     FFHTFNTLHN ASKQVVITSD LPPKQLNGFE DRMRSRFEWG LITDVQPPDL ETRIAILRKK
     AASERLQAPD DVLEYIASRI STNIRELEGA LIRVTAFANL NRQLVDVSLA EIVLKDLITD
     DQTQEITATT VIGQTAAYFG LSIEDLCGSS RSRVLVTARQ IAMYLCRELT DLSLPKIGQA
     FGGRDHTTVM HANRKIRELM AERRSIYNQV TELTNRIKQQ HRG
//
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