ID   ATPL_SULAC              Reviewed;         101 AA.
AC   Q4J8L5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Membrane-associated ATPase C chain;
GN   Name=atpP; OrderedLocusNames=Saci_1552;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: The C chain is a proteolipid, and one of the membranous
CC       subunits of the nonenzymatic component of the Sul-ATPase complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CP000077; AAY80865.1; -; Genomic_DNA.
DR   RefSeq; WP_011278367.1; NC_007181.1.
DR   AlphaFoldDB; Q4J8L5; -.
DR   SMR; Q4J8L5; -.
DR   STRING; 330779.Saci_1552; -.
DR   EnsemblBacteria; AAY80865; AAY80865; Saci_1552.
DR   GeneID; 3474587; -.
DR   KEGG; sai:Saci_1552; -.
DR   PATRIC; fig|330779.12.peg.1492; -.
DR   eggNOG; arCOG02455; Archaea.
DR   HOGENOM; CLU_148047_3_1_2; -.
DR   OMA; MTKYNKI; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   Gene3D; 1.20.120.610; -; 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; SSF81333; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Hydrogen ion transport; Hydrolase;
KW   Ion transport; Lipid-binding; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..101
FT                   /note="Membrane-associated ATPase C chain"
FT                   /id="PRO_0000071732"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   101 AA;  9949 MW;  FC4A3FDB3600A917 CRC64;
     MRKALLISLI LPILIGGLVA AAQAPQDTPQ GFMGINIGAG LAVGLAAIGA GVAVGTAAAA
     GIGVLTEKRE MFGTVLIFVA IGEGIAVYGI IFAVLMLFAG I