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Database: UniProt
Entry: A0A1M4U510_9CLOT
LinkDB: A0A1M4U510_9CLOT
Original site: A0A1M4U510_9CLOT 
ID   A0A1M4U510_9CLOT        Unreviewed;       164 AA.
AC   A0A1M4U510;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=V/A-type H+-transporting ATPase subunit K {ECO:0000313|EMBL:SHE51743.1};
GN   ORFNames=SAMN05443638_10437 {ECO:0000313|EMBL:SHE51743.1};
OS   Clostridium fallax.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1533 {ECO:0000313|EMBL:SHE51743.1, ECO:0000313|Proteomes:UP000184035};
RN   [1] {ECO:0000313|EMBL:SHE51743.1, ECO:0000313|Proteomes:UP000184035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2631 {ECO:0000313|EMBL:SHE51743.1,
RC   ECO:0000313|Proteomes:UP000184035};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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, ECO:0000256|RuleBase:RU363060}.
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DR   EMBL; FQVM01000004; SHE51743.1; -; Genomic_DNA.
DR   RefSeq; WP_072893053.1; NZ_UAVV01000002.1.
DR   AlphaFoldDB; A0A1M4U510; -.
DR   STRING; 1533.SAMN05443638_10437; -.
DR   OrthoDB; 384481at2; -.
DR   Proteomes; UP000184035; 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; cd18179; ATP-synt_Vo_Ao_c_NTPK_rpt1; 1.
DR   CDD; cd18180; ATP-synt_Vo_Ao_c_NTPK_rpt2; 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   PANTHER; PTHR10263:SF18; V-TYPE PROTON ATPASE 21 KDA PROTEOLIPID SUBUNIT C; 1.
DR   PANTHER; PTHR10263; V-TYPE PROTON ATPASE PROTEOLIPID SUBUNIT; 1.
DR   Pfam; PF00137; ATP-synt_C; 2.
DR   PRINTS; PR00122; VACATPASE.
DR   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 2.
PE   3: Inferred from homology;
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU363060};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363060};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184035};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU363060};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU363060};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363060}.
FT   TRANSMEM        60..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        93..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   TRANSMEM        139..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363060"
FT   DOMAIN          20..79
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
FT   DOMAIN          100..159
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
SQ   SEQUENCE   164 AA;  17050 MW;  D5BEBC6AA5C6198C CRC64;
     MNTWIEFFAN GTNGMIFALL GAAIAVGLAG IGSAQGIGIV GQAAAGLMAE DPDKFGKTFI
     LVALPGTQGL YGFVIALLLF TKIGIFGGDA PELGLGLKYF MACLPVAIAG WRSAIWQGKV
     AAAGVQILAK RPNDVMKGVI YAVMVETYAV LGFVASLFMV LFIK
//
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