ID A0A099WQY4_PORCN Unreviewed; 621 AA.
AC A0A099WQY4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=V-type ATP synthase subunit I {ECO:0000256|RuleBase:RU361189};
GN ORFNames=HQ35_00200 {ECO:0000313|EMBL:KGN83230.1};
OS Porphyromonas cangingivalis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=36874 {ECO:0000313|EMBL:KGN83230.1, ECO:0000313|Proteomes:UP000030125};
RN [1] {ECO:0000313|EMBL:KGN83230.1, ECO:0000313|Proteomes:UP000030125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COT-109 OH1386 {ECO:0000313|Proteomes:UP000030125};
RA Wallis C., Deusch O., O'Flynn C., Davis I., Jospin G., Darling A.E.,
RA Coil D.A., Alexiev A., Horsfall A., Kirkwood N., Harris S., Eisen J.A.;
RT "Porphyromonas cangingivalis strain:COT-109_OH1386 Genome sequencing.";
RL Submitted (AUG-2014) 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 116 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00009904, ECO:0000256|RuleBase:RU361189}.
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:KGN83230.1}.
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DR EMBL; JQJD01000001; KGN83230.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099WQY4; -.
DR STRING; 36874.HQ34_10040; -.
DR eggNOG; COG1269; Bacteria.
DR Proteomes; UP000030125; 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 InterPro; IPR002490; V-ATPase_116kDa_su.
DR PANTHER; PTHR11629:SF63; V-TYPE PROTON ATPASE SUBUNIT A; 1.
DR PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR Pfam; PF01496; V_ATPase_I; 1.
PE 3: Inferred from homology;
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361189};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361189};
KW Reference proteome {ECO:0000313|Proteomes:UP000030125};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361189};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361189};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361189}.
FT TRANSMEM 333..358
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 370..393
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 413..435
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 447..465
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 477..496
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 503..522
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 528..550
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
FT TRANSMEM 562..586
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361189"
SQ SEQUENCE 621 AA; 69738 MW; 0A13F6973C793E59 CRC64;
MIIKMNKYSF LIFHKEYSDF LVRLRDLGVV HIRQNNDTKQ VEEIKALLAE QKQIRATIDR
MNTMWSSAGI TADDLKPVSE YLHVSHDSFS TAQKYIETIA TIDTEIETNQ KKVNELNQLK
GELKIWGDFD PQLLKRLADA GQEIRFWSVP LPQYKPEWEE LYGAIIISDA RRIASFVTVT
PTGMSPKISA EKVDLPMRSL SDIEREISEI TEETARLRES LVYLSHDKSV MERHLSELED
VYNMSNALLQ GEAMFDDALI VLEGYIPAEQ SEDLEKALDT EGYAYTQLEI KETDDVPVKL
KNNFFVKVFE PIVKLFSLPN YHEIDPTPFV APFFMLFFAM CFGDAGYGLF LLILCSIFKV
KAKDNLKPVL SLFQWLGGAA AVIGFFSGSF FGIELAKVEA LAAVRQFFIS SDNMMIIAIA
VGLVQIIVAK FVGAYKVKVQ KGTRHALSPF AWVIFIIVML AIVLFGLPQV DLQLPTYVNY
ILYGIAGCCA VIMLFFNSPG KSIFFNIGSS LWTAYNTASG LLGDSLSYIR LFAIGLTGAI
LGNVFNTLAI SMTDGIPMYV RWLPMLIILL IGHTINFGLA MIGSLVHPVR LIFVEYFNNS
DFEGGGQAYA PLKKNSLTQD Q
//