ID A0A0A2XD65_THEFI Unreviewed; 98 AA.
AC A0A0A2XD65;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=ATP synthase subunit K {ECO:0000313|EMBL:KGQ23089.1};
GN ORFNames=THFILI_09495 {ECO:0000313|EMBL:KGQ23089.1};
OS Thermus filiformis.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=276 {ECO:0000313|EMBL:KGQ23089.1, ECO:0000313|Proteomes:UP000030364};
RN [1] {ECO:0000313|EMBL:KGQ23089.1, ECO:0000313|Proteomes:UP000030364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43280 {ECO:0000313|EMBL:KGQ23089.1,
RC ECO:0000313|Proteomes:UP000030364};
RA Mandelli F., Ramires B.O., Paixao D.A., Camilo C.M., Polikarpov I.,
RA Couger M.B., Prade R., Riano-Pachon D.M., Squina F.M.;
RT "Draft Genome Sequence of the thermophile Thermus filiformis ATCC43280
RT producer of carotenoid-(di)glucoside-branched fatty acids (di)esters.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000256|ARBA:ARBA00007296}.
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:KGQ23089.1}.
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DR EMBL; JPSL02000040; KGQ23089.1; -; Genomic_DNA.
DR RefSeq; WP_038060333.1; NZ_JPSL02000040.1.
DR AlphaFoldDB; A0A0A2XD65; -.
DR STRING; 276.THFILI_09495; -.
DR PATRIC; fig|276.5.peg.57; -.
DR OrthoDB; 27598at2; -.
DR Proteomes; UP000030364; Unassembled WGS sequence.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd18181; ATP-synt_Vo_Ao_c_TtATPase_like; 1.
DR Gene3D; 1.20.120.610; lithium bound rotor ring of v- atpase; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..98
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001997020"
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..94
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 98 AA; 9621 MW; EB75CB0600BA0306 CRC64;
MKKLGVIFAV ILGALAFAAE EAAASGGLDR GLIAVGMGLA VGLAALGTGV AQARIGAAGV
GAVAEDRGNF GTALIFLLLP ETLVIFGLLI AFILNGKL
//
