VATI1_TREPA
ID VATI1_TREPA Reviewed; 622 AA.
AC O83444;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=V-type ATP synthase subunit I 1;
DE AltName: Full=V-ATPase subunit I 1;
GN Name=atpI1; OrderedLocusNames=TP_0429;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AE000520; AAC65415.1; -; Genomic_DNA.
DR PIR; B71326; B71326.
DR RefSeq; WP_010881877.1; NC_021490.2.
DR AlphaFoldDB; O83444; -.
DR SMR; O83444; -.
DR STRING; 243276.TPANIC_0429; -.
DR TCDB; 3.A.2.3.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR EnsemblBacteria; AAC65415; AAC65415; TP_0429.
DR KEGG; tpa:TP_0429; -.
DR eggNOG; COG1269; Bacteria.
DR HOGENOM; CLU_025558_1_1_12; -.
DR OMA; INESYAW; -.
DR OrthoDB; 259071at2; -.
DR Proteomes; UP000000811; 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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR PANTHER; PTHR11629; PTHR11629; 2.
PE 3: Inferred from homology;
KW Cell membrane; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..622
FT /note="V-type ATP synthase subunit I 1"
FT /id="PRO_0000119242"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 622 AA; 69077 MW; 2AECAD4E47821C91 CRC64;
MIVPMKKVTL LVLGSEQERS LQALRSFGAV HVQLRECASE QLAELHALDA RCVQAIALVT
DAQTKNVTRG EECRVAGQVV EAAEAVEQIV RTHSDRVELA QRIAQCIAHL ERCEPWGDFD
PADVRALAQR GIHLIPVELS ERSYRCLPDE LQTLCLARRG GLVRCVLVAD KPGLPPSLPA
DARALELPDV SPADLFVRLR QLREECATLT QRLLAYSEYQ GAIRALRQKI AADIEFERVH
LSMVSVDVSQ WRETGETLRI AHVSGYLPVS RVRAFSECAR KEAWAYCCVD PMPEDPVPTQ
LRNNRWVNLI SPLMNFLGTV PGYWEVDISG FFLLFFGVFF SIIFADAGYG AVLTLVSLGG
IVLSKRKHAV VSPAWCLGLY LGTLTMVWGA LVCNWFGVPV QYVPASLARI AVWEISGFAD
AAQRNKNQMH VCFFLGLLHL CLGHLIVVRR TFRSLRVLAE FGSLLMLGGM YVVVLNLIVD
KERYPLTGMI VGSIIAGFVL NFIFVNYRVS VRQSVADSMK NVINALLGIV NVFADVMSYI
RLWAVGLAGG AISATVNEMT HPLFANFLAF LGIVLLLFGH GLNYVMSILS VIVHGVRLNT
LEFSNHVGLM WTGIRYTPFR ER