ID A0A0U5AVM3_9BACT Unreviewed; 427 AA.
AC A0A0U5AVM3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=ATPase AAA {ECO:0000313|EMBL:BAU22415.1};
GN ORFNames=THC_0007 {ECO:0000313|EMBL:BAU22415.1};
OS Caldimicrobium thiodismutans.
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae; Caldimicrobium.
OX NCBI_TaxID=1653476 {ECO:0000313|EMBL:BAU22415.1, ECO:0000313|Proteomes:UP000068196};
RN [1] {ECO:0000313|EMBL:BAU22415.1, ECO:0000313|Proteomes:UP000068196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF1 {ECO:0000313|EMBL:BAU22415.1,
RC ECO:0000313|Proteomes:UP000068196};
RX PubMed=26842785; DOI=10.1099/ijsem.0.000947;
RA Kojima H., Umezawa K., Fukui M.;
RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT bacterium isolated from a hot spring, and emended description of the genus
RT Caldimicrobium.";
RL Int. J. Syst. Evol. Microbiol. 66:1828-1831(2016).
RN [2] {ECO:0000313|Proteomes:UP000068196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF1 {ECO:0000313|Proteomes:UP000068196};
RA Kojima H., Umezawa K., Fukui M.;
RT "Caldimicrobium thiodismutans sp. nov., a sulfur-disproportionating
RT bacterium isolated from a hot spring.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2016).
CC -!- SIMILARITY: Belongs to the AAA ATPase family. RarA/MGS1/WRNIP1
CC subfamily. {ECO:0000256|ARBA:ARBA00008959}.
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DR EMBL; AP014945; BAU22415.1; -; Genomic_DNA.
DR RefSeq; WP_068511522.1; NZ_AP014945.1.
DR AlphaFoldDB; A0A0U5AVM3; -.
DR STRING; 1653476.THC_0007; -.
DR KEGG; cthi:THC_0007; -.
DR PATRIC; fig|1653476.3.peg.7; -.
DR OrthoDB; 9778364at2; -.
DR Proteomes; UP000068196; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd18139; HLD_clamp_RarA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 1.10.3710.10; DNA polymerase III clamp loader subunits, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032423; AAA_assoc_2.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR InterPro; IPR021886; MgsA_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13779:SF7; ATPASE WRNIP1; 1.
DR PANTHER; PTHR13779; WERNER HELICASE-INTERACTING PROTEIN 1 FAMILY MEMBER; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF16193; AAA_assoc_2; 1.
DR Pfam; PF12002; MgsA_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000068196}.
FT DOMAIN 37..155
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT COILED 69..96
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 427 AA; 48292 MW; 0FFD3FA6BC1E8979 CRC64;
MASLSERLRP RSLKEFVGQR HLFEKGGTLY YLLKREKPFS LIFWGPPGTG KTTLSYLLGK
YFQAHFVAVS AVDTTLKDLK DLIKQAENLK KLGKNTILFI DEIHRFNKAQ QAFLLPYVEK
ELIFLFGATT ENPSFEIIAP LLSRVRVLQL YPLEEDEILQ LLKRALIDET NGYGTYNYIV
KDEVLKTIAQ ASQGDGRFAL NTLEILVEGA IQEGLKEITL EALTQNLLTK PLLYDKSGEE
HYNLISAFHK SMRGSDPDAT IYWMVRMLEA GEDPLYIARR ILICAAEDVG LADPLALVVA
LSAFKAYEIL GSPEGEIALA EAALYVALAP KSNSSYLALK KAKDLIKKTG AQPVPLHLRN
PVTALMEKMG YGKDYQYPHD FEHAFVLQEY LPEALKKIIF YQPKEIGVES TFKERLKKLW
GKYKGYV
//
