ID A0PLB6_MYCUA Unreviewed; 777 AA.
AC A0PLB6;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=Metal cation transporter P-type ATPase, CtpV {ECO:0000313|EMBL:ABL03135.1};
GN Name=ctpV {ECO:0000313|EMBL:ABL03135.1};
GN OrderedLocusNames=MUL_0423 {ECO:0000313|EMBL:ABL03135.1};
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL03135.1, ECO:0000313|Proteomes:UP000000765};
RN [1] {ECO:0000313|EMBL:ABL03135.1, ECO:0000313|Proteomes:UP000000765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99 {ECO:0000313|EMBL:ABL03135.1,
RC ECO:0000313|Proteomes:UP000000765};
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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 IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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DR EMBL; CP000325; ABL03135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0PLB6; -.
DR KEGG; mul:MUL_0423; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_11; -.
DR Proteomes; UP000000765; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd02094; P-type_ATPase_Cu-like; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR006121; HMA_dom.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362081};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 151..170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 210..228
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 234..251
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 385..407
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 413..440
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..66
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 777 AA; 81019 MW; 98085CA68C6E5D65 CRC64;
MRVHANGFAI DATRAAAIEE SVGRVGGVRA VRAYPRTASV VIWYSPAHCD TAAIVSAIAE
AEHAGDASAP APAARVAGIA DGGVVGRVIG GLARALLGMR TDDNDDDPPP EIARLRAALD
RIGYSPEQDT ATQLSPSEQA RSGIRFWSRR AWLAWPLGLL ASGLTMFFGA YPWAGWLAFA
ATIPVQFIAG WPFLVGAVQQ ARARSANMNT LISLGTLTAF IYSTYQLFAG GPLFFDTAAL
IIAFVVLGRY FEATAHGKTR EAISKLLDMG AKETRLIVDG EEHLVPVDRV QVGDLVRVRP
GEKIPVDGEV IDGRAAVDES MLTGESVPVE KGVGDWVAGA TVNTDGLLTV RATAVGADTA
LAQIVRLVEE AQGGKAPVQR LADRVSAVFV PVVVRIAAAT FAGWTLLAAN PVAGMTAAVS
VLIIACPYAL GLATPTAIIV GTGRGADMGI LVKGGEVLEA SKKIDTVVFD KTGTLTRAQM
ELTDVIAGKR RQPDVVLRIA AAVESGSEHP IGAAIVAGAR ERELEVPPAT EFTNLAGHGV
RGEVGGKSVL VGRRKLVDEQ HLRLPEQLAA AAADLEERGR TAVYVGQDGQ VVGVLAVADT
VKDDAADVVS QLHAMGLQVA LITGDNARTA AAIAAQVGID RVLAEVLPAD KVNEVRRLQD
EGRIVAMVGD GVNDAPALVQ ADLGIAIGTG TDVAIEASDI TLMSGRLDGV VSAIELSRRT
LRTIYQNLGW AFGYNTAAIP LAALGVLNPV VAGAAMGLSS VSVVTNSLRL RRFGRDV
//
