ID E8T6V8_THEA1 Unreviewed; 387 AA.
AC E8T6V8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=ATPase associated with various cellular activities AAA_5 {ECO:0000313|EMBL:ADU97781.1};
GN OrderedLocusNames=Theam_1825 {ECO:0000313|EMBL:ADU97781.1};
OS Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1).
OG Plasmid pTHEAM01 {ECO:0000313|EMBL:ADU97781.1,
OG ECO:0000313|Proteomes:UP000006362}.
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Thermovibrio.
OX NCBI_TaxID=648996 {ECO:0000313|EMBL:ADU97781.1, ECO:0000313|Proteomes:UP000006362};
RN [1] {ECO:0000313|EMBL:ADU97781.1, ECO:0000313|Proteomes:UP000006362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15698 / JCM 12110 / HB-1
RC {ECO:0000313|Proteomes:UP000006362};
RC PLASMID=pTHEAM01 {ECO:0000313|EMBL:ADU97781.1,
RC ECO:0000313|Proteomes:UP000006362};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Vetriani C., Woyke T.;
RT "Complete sequence of plasmid of Thermovibrio ammonificans HB-1.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CbbQ/NirQ/NorQ/GpvN family.
CC {ECO:0000256|ARBA:ARBA00009417}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002445; ADU97781.1; -; Genomic_DNA.
DR RefSeq; WP_013524985.1; NC_014917.1.
DR AlphaFoldDB; E8T6V8; -.
DR KEGG; tam:Theam_1825; -.
DR eggNOG; COG0714; Bacteria.
DR HOGENOM; CLU_713575_0_0_0; -.
DR OrthoDB; 9808317at2; -.
DR Proteomes; UP000006362; Plasmid pTHEAM01.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR InterPro; IPR013615; CbbQ_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007527; Znf_SWIM.
DR PANTHER; PTHR42759:SF1; MAGNESIUM-CHELATASE SUBUNIT CHLD; 1.
DR PANTHER; PTHR42759; MOXR FAMILY PROTEIN; 1.
DR Pfam; PF07728; AAA_5; 1.
DR Pfam; PF08406; CbbQ_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Plasmid {ECO:0000313|EMBL:ADU97781.1};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00325};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00325}.
FT DOMAIN 43..87
FT /note="SWIM-type"
FT /evidence="ECO:0000259|PROSITE:PS50966"
SQ SEQUENCE 387 AA; 42593 MW; 9DBE5CA049C1EC2E CRC64;
MAVKVVEPND YRYKNGKTRS QAGKELLRKA EILDESLVAP GTYRVVYDGK EHTVRYDGSS
WSCDCEDQRS RAKGGCKHIW AVYWAMAAGV IEPPEELPKK VKLSGGPKAS AKAEVKTEGF
VGPQKGQLLT ALKLNKNALL KGPTGTGKTV LVREVAKELG YKLGYVAGSE SLQDIDFLGA
FVKKGDSIEW VDGKLTKAFR LAQKGRVILF IDEINRIPSK HLNILIGVMN PSGGKYTLYN
HLTGETIEAP IENLRFIGAM NEGGAYQVHP LDPALMRRFE SKIQFYYLPP ELEAGLIVKR
TGLSKEVAEK MVKVANLQRE AVKRGEYDFP LDTASLLNWA EMVVKGGLSP EEAAACTWLY
GLVGAEMDGT PNEEQVAGLK KLIETVF
//
