ID A0A1M4N5S3_9CLOT Unreviewed; 160 AA.
AC A0A1M4N5S3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Sodium ATPase proteolipid component {ECO:0000313|EMBL:SCN21654.1};
GN Name=ntpK {ECO:0000313|EMBL:SCN21654.1};
GN ORFNames=N3C_0348 {ECO:0000313|EMBL:SCN21654.1};
OS Clostridium sp. N3C.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1776758 {ECO:0000313|EMBL:SCN21654.1, ECO:0000313|Proteomes:UP000184869};
RN [1] {ECO:0000313|EMBL:SCN21654.1, ECO:0000313|Proteomes:UP000184869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N3C {ECO:0000313|EMBL:SCN21654.1};
RA Seilhamer J.J.;
RL Submitted (AUG-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; FMJL01000003; SCN21654.1; -; Genomic_DNA.
DR RefSeq; WP_074364358.1; NZ_FMJL01000003.1.
DR AlphaFoldDB; A0A1M4N5S3; -.
DR STRING; 1776758.N3C_0348; -.
DR OrthoDB; 384481at2; -.
DR Proteomes; UP000184869; 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:UP000184869};
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 57..80
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 92..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT TRANSMEM 133..156
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363060"
FT DOMAIN 19..77
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
FT DOMAIN 95..154
FT /note="V-ATPase proteolipid subunit C-like"
FT /evidence="ECO:0000259|Pfam:PF00137"
SQ SEQUENCE 160 AA; 16684 MW; 2F8453F327C2B599 CRC64;
MNFVQFLFEN NGGFILAVLG VALAVGMAGV GSAKGVGLVG QAAAGLMTEQ PEKFGKSLVL
ELLPGTQGLY GFVIGLLVFL RIDANISLQQ GLYYLMACLP IAIVGLWSAI AQGKAAAAGI
AILAKKPEHN IKGIIYAAMV ETYALLGFVM SMLLVFSANF
//
