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Database: UniProt
Entry: D5P483_9MYCO
LinkDB: D5P483_9MYCO
Original site: D5P483_9MYCO 
ID   D5P483_9MYCO            Unreviewed;       821 AA.
AC   D5P483;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Plasma-membrane proton-efflux P-type ATPase {ECO:0000313|EMBL:EFG79080.1};
DE            EC=3.6.3.6 {ECO:0000313|EMBL:EFG79080.1};
GN   Name=gltX {ECO:0000313|EMBL:EFG79080.1};
GN   ORFNames=HMPREF0591_0977 {ECO:0000313|EMBL:EFG79080.1};
OS   Mycobacterium parascrofulaceum ATCC BAA-614.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium simiae complex.
OX   NCBI_TaxID=525368 {ECO:0000313|EMBL:EFG79080.1, ECO:0000313|Proteomes:UP000003653};
RN   [1] {ECO:0000313|EMBL:EFG79080.1, ECO:0000313|Proteomes:UP000003653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-614 {ECO:0000313|EMBL:EFG79080.1,
RC   ECO:0000313|Proteomes:UP000003653};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIIA subfamily. {ECO:0000256|ARBA:ARBA00008804}.
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:EFG79080.1}.
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DR   EMBL; ADNV01000083; EFG79080.1; -; Genomic_DNA.
DR   AlphaFoldDB; D5P483; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_6_4_11; -.
DR   Proteomes; UP000003653; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008553; F:P-type proton-exporting transporter activity; IEA:InterPro.
DR   GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR   CDD; cd02076; P-type_ATPase_H; 1.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR006534; P-type_ATPase_IIIA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01647; ATPase-IIIA_H; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF31; PLASMA MEMBRANE ATPASE-RELATED; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000313|EMBL:EFG79080.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        54..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        669..694
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        737..761
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        767..784
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..78
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   821 AA;  87721 MW;  FC984F69CF142D06 CRC64;
     MDAEHRHIRG DGLTHASEFT GTSTGLTTAE AQQRLQRYGP NEIAERHRNP VLEFLGYFWA
     PIPWMIEVAL ALSVAARHWT DAAIIGVLLA MNGLVAFFEE HQAANAIAAL KQRLATSARA
     LRDGAWVTVP VRELVPGDVV RVRLGDVMPA DLRVLDDATL EVDQSALTGE SLAVSRGRGQ
     DLFSGSVLVR GEADALVCAT GASSYMGKTT ALVESAGTVS HFQRAVLRIG NYLILIAVAL
     VTLAVVVSLV RGNPVLQTLE FALVVTIASI PVALPAVLSV TMAIGARQLA RQQAVVSHLP
     AVEELGGIDL LCSDKTGTLT QNRLAVADRW TAAAVSDDEL LEVAALASRA EDNDLIDLAV
     MAAAGQLPAA RVDQFVPFDP VTKRTEAMVR HSDGQTFRVS KGAPQVIAAL CDGDAAANEI
     NDVVERFATR GHRSLGVAKT DGDGSWRLMG VLALADPPRD DSAATIAAAK ELGIDVKMVT
     GDQVAIGREI ARQVGLGEQI LDAAVLDTAA DEDDLGAHVE ATDGFAQVFP EHKYHIVRLL
     QARGHIVGMT GDGVNDAPAL KQADAGIAVS GATDAARAAA DVVLLAPGLS VIVAAIRQAR
     EIFARMTSYA TYRIAETIRV LLLITLAIVF MNFFPVTAVM IVFLALLNDG AILAIAYDHV
     RGSAKPASWD MRSVLTIATA LGTMGVAETF LLFALADNTF QLNHDLIRTL IYLKLSVSGH
     LTVFVTRTRH PFWSRPAPAR ILLAAVIGTQ VIATLIAVYG MAMTPLGWRW AGIVWAYALF
     WFLIEDRVKL GAYHWLDHHP RREHPSDPLP VADSPPRAGG L
//
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