ID   A0A1H8KIG7_9FIRM        Unreviewed;       161 AA.
AC   A0A1H8KIG7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=V/A-type H+-transporting ATPase subunit K {ECO:0000313|EMBL:SEN92743.1};
GN   ORFNames=SAMN05216454_1321 {ECO:0000313|EMBL:SEN92743.1};
OS   Peptostreptococcus russellii.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Peptostreptococcus.
OX   NCBI_TaxID=215200 {ECO:0000313|EMBL:SEN92743.1, ECO:0000313|Proteomes:UP000199512};
RN   [1] {ECO:0000313|EMBL:SEN92743.1, ECO:0000313|Proteomes:UP000199512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Calf135 {ECO:0000313|EMBL:SEN92743.1,
RC   ECO:0000313|Proteomes:UP000199512};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FODF01000032; SEN92743.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8KIG7; -.
DR   STRING; 215200.SAMN05216454_1321; -.
DR   OrthoDB; 384481at2; -.
DR   Proteomes; UP000199512; Unassembled WGS sequence.
DR   GO; GO:0033177; C:proton-transporting two-sector ATPase complex, proton-transporting domain; IEA:InterPro.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; 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; 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   SUPFAM; SSF81333; F1F0 ATP synthase subunit C; 2.
PE   3: Inferred from homology;
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199512};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        90..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..76
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
FT   DOMAIN          94..152
FT                   /note="V-ATPase proteolipid subunit C-like"
FT                   /evidence="ECO:0000259|Pfam:PF00137"
SQ   SEQUENCE   161 AA;  16552 MW;  CF429C343696AB2B CRC64;
     MNFGSWIVEN GGVVFGGLGV VFAMLSALGS AKGLSIVGQA ASGLVPEEPQ KFGKTLILQL
     LPGTQGLYGF VIGLLILLKL NGDIGLAQGM YLAAVGMPIG FVGWGSAVSQ GKVAASGVGI
     LAKNEAQTTK GIIYSVMVET YALLAFVISL LLFFKFGAFF A
//