ID P96271_MYCTU Unreviewed; 1539 AA. AC P96271; I6Y7S5; L0T3N8; DT 01-MAY-1997, integrated into UniProtKB/TrEMBL. DT 01-MAY-1997, sequence version 1. DT 27-MAR-2024, entry version 158. DE SubName: Full=Possible metal cation transporting P-type ATPase CtpH {ECO:0000313|EMBL:CCP43156.1}; GN Name=ctpH {ECO:0000313|EMBL:CCP43156.1}; GN OrderedLocusNames=Rv0425c {ECO:0000313|EMBL:CCP43156.1}; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332 {ECO:0000313|EMBL:CCP43156.1, ECO:0000313|Proteomes:UP000001584}; RN [1] {ECO:0000313|EMBL:CCP43156.1, ECO:0000313|Proteomes:UP000001584} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv {ECO:0000313|Proteomes:UP000001584}; RX PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E.III., Tekaia F., Badcock K., RA Basham D., Brown D., Chillingworth T., Connor R., Davies R., Devlin K., RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., RA Krogh A., McLean J., Moule S., Murphy L., Oliver K., Osborne J., RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton J., RA Squares R., Squares S., Sulston J.E., Taylor K., Whitehead S., RA Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the complete RT genome sequence."; RL Nature 393:537-544(1998). RN [2] {ECO:0007829|PubMed:21969609} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21969609; DOI=10.1074/mcp.M111.011445; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K., RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R., RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M., RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution RT mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000256|ARBA:ARBA00001836}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL123456; CCP43156.1; -; Genomic_DNA. DR RefSeq; NP_214939.1; NC_000962.3. DR RefSeq; WP_003911174.1; NZ_NVQJ01000002.1. DR AlphaFoldDB; P96271; -. DR SMR; P96271; -. DR STRING; 83332.Rv0425c; -. DR PaxDb; 83332-Rv0425c; -. DR GeneID; 886373; -. DR KEGG; mtu:Rv0425c; -. DR PATRIC; fig|83332.111.peg.466; -. DR eggNOG; COG0474; Bacteria. DR InParanoid; P96271; -. DR OrthoDB; 9814270at2; -. DR PhylomeDB; P96271; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0005829; C:cytosol; HDA:MTBBASE. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0005388; F:P-type calcium transporter activity; IBA:GO_Central. DR CDD; cd07539; P-type_ATPase; 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; IPR006068; ATPase_P-typ_cation-transptr_C. DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N. 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; IPR001757; P_typ_ATPase. DR InterPro; IPR044492; P_typ_ATPase_HD_dom. 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; PF00689; Cation_ATPase_C; 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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1. PE 1: Evidence at protein level; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001584}; 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 1409..1432 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 1444..1463 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1313..1463 FT /note="Cation-transporting P-type ATPase C-terminal" FT /evidence="ECO:0000259|Pfam:PF00689" FT REGION 1469..1539 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1470..1484 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1515..1529 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1539 AA; 159773 MW; 27F76F9F0EB9FACF CRC64; MPVRAVATGF RATATLTGAS ITAATAVSAT LAKTGVGTGM KVAIIPLRAG AKALSGELSR ETLGRNCWRG ERRAWIEVRG LRSGGDDELG RVVLNAIQAH PGVGSASLNY PLSRVVVAID DPDTSLRELC RIVDDAEKAE RHRHPDQAAD QLAQSPGSLP GDGVLLAVRA VTVAATAAGL GLALGGRALR WPRFPLVIEA AVAAVDHQPL LRRLLEDRIG TEATATVLEL AMAAAHTVTL SPAALSVDLT IQALKAAECR AGARAWRRHE PQLALHADEP ADQPQSLWPR PARSTQPVQR SVARFALIQA LSAVLVGAGT RDADMAATAT LVATPKASRT TPEAFAAALG QGLADQHAVL PLRPESLRRL DRVDAIVIDP RVLCTDDLRV ARIRGCGADE LSTAWNRAQL VLTESGLRPG WHRVPGVSAS GSDSAVEALF RPMHDRLASA VVAEAHRTGA DLVSVDVDAL GELRPVFDDI RPLDDGASGS LDEALARAVA ELRQAGRTVA VLSSVGKQAL SAADVALGVL PPPGAGAPPW YADVLLPDLG AAWRVLHAIP AARAARQRGN EISGGASALG ALLMLPGVRG LGPGPVTTGA AAGLLSGYLL ARKVVDAQAP RPAPAHEWHA MSVEQVRKAL PSPDEQAPAK APPSPYPARA LAGGLHTAKR GAQITQAPLN ALWQLTKAMR AELSDPLTPM LALGAMASAV LGSPVDAVMV GSVLTGNSIL AASQRLRAES RLNRLLAQQI PPARKVLAGA DDQPRYIEVR AEELRPGDII EVRTHEVVPA DARVIEEVDV EVDESALTGE SLSVTKQVEP TPGVDLIERR CMLYAGTTVV SGTAVAVVTA VGPDTQERRA AELVSGDLSS VGLQHQLSRL TNQAWPVSMT GGALVTGLGL LRRRGLRQAV ASGIAVTVAA VPEGMPLVAT LAQQASARRL SHFGALVRIP RSVEALGRVD MVCFDKTGTL SENRLRVAQV RPVAGHSREE VLRCAAHAAP ASNGPQVHAT DVAIVQAAAA AAASGTDGAE PGAAEPAAHL PFRSGRSFSA SVSGTELTVK GAPEVVLAAC EGIGSSMDDA VAELAANGLR VIAVAHRQLT AQQAQSVVDD PDEIARLCRD ELSLVGFLGL SDTPRAQAAA LLADLHEHDL DIRLITGDHP ITAAAIAEEL GMQVSPEQVI SGAEWDALSR KDQERAVAER VIFARMTPEN KVQIVQTLEH SGRVCAMVGD GSNDAAAIRA ATVGIGVVAH GSDPARVAAD LVLVDGRIES LLPAILEGRQ LWQRVQAAVS VLLGGNAGEV AFAIIGSAIT GTSPLNTRQL LLVNMLTDAL PAAALAVSKP SDPVTPATRG PDQRELWRAV GIRGATTAAA ATVAWVMAGF TGLPRRASTV ALVALVAAQL GQTLVDSHAW LVVLTALGSL AALATLISIP VVSQLLGCTP LDPLGWAQAT AAATAATVAV AVLNRVLTGR DKSGQPNPQP PETDALSRDA SPGAPPGPRR RRRATARRKA PVKAPSATRQ TTKPKGPPAH RSSSTYPRR //