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P46839 (CTPA_MYCLE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cation-transporting P-type ATPase A
EC=3.6.3.-
Gene names
Name:ctpA
Ordered Locus Names:ML1987
OrganismMycobacterium leprae [Complete proteome] [HAMAP]
Taxonomic identifier1769 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + H2O = ADP + phosphate.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily. [View classification]

Contains 1 HMA domain.

Sequence caution

The sequence CAA86358.1 differs from that shown. Reason: Frameshift at positions 43, 57, 360 and 377.

The sequence CAC30942.1 differs from that shown. Reason: Frameshift at position 16.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processATP biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

copper-exporting ATPase activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 780780Cation-transporting P-type ATPase A
PRO_0000046164

Regions

Topological domain1 – 8888Cytoplasmic Potential
Transmembrane89 – 11022Helical; Potential
Topological domain111 – 1199Extracellular Potential
Transmembrane120 – 13920Helical; Potential
Topological domain140 – 1467Cytoplasmic Potential
Transmembrane147 – 16721Helical; Potential
Topological domain168 – 19427Extracellular Potential
Transmembrane195 – 21521Helical; Potential
Topological domain216 – 344129Cytoplasmic Potential
Transmembrane345 – 36723Helical; Potential
Topological domain368 – 3747Extracellular Potential
Transmembrane375 – 39218Helical; Potential
Topological domain393 – 678286Cytoplasmic Potential
Transmembrane679 – 69820Helical; Potential
Topological domain699 – 7035Extracellular Potential
Transmembrane704 – 72219Helical; Potential
Topological domain723 – 78058Cytoplasmic Potential
Domain3 – 6866HMA

Sites

Active site43014-aspartylphosphate intermediate By similarity
Metal binding131 Potential
Metal binding161 Potential
Metal binding6241Magnesium By similarity
Metal binding6281Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
P46839 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: BCA853E957F15C78

FASTA78081,791
        10         20         30         40         50         60 
MQRIQLNITG MSCSCCAPNG WNNLPNKLSD FSTLVNSATR VAAINLSEVT QTAEVCEAVR 

        70         80         90        100        110        120 
RAALCTDGGE ALQRRQADAD NARYLLIRLA VAAALFVPLA HLSVMFAVLP STHFPGWEWM 

       130        140        150        160        170        180 
LTALAIPVVT WAAWPFHRVA IHNARYHGAS METLISTGIT AATIWSLYTV FGHHQSTEHR 

       190        200        210        220        230        240 
GVWRALLGSD AIYFEVAAGI TVFVLAGKYY TARAKSHASI ALLALAALSA KDAAVLQPDG 

       250        260        270        280        290        300 
SEMVIPANEL NEQQRFVVRP GQTIAADGLV IDGSATVSMS PITGEAKPVR VNPGAQVIGG 

       310        320        330        340        350        360 
TVVLNGRLIV EAAAVGDETQ LAGMVRLVEQ AQQQNANAQR LADRIASVFV PCVFAVAALT 

       370        380        390        400        410        420 
AVGWLIAGSG PDRVFSAAIA VLVIACPCAL GLATPTAMMV ASGRGAQLGI LLKGHESFEA 

       430        440        450        460        470        480 
TRAVDTVVFD KTGTLTTGQL KVSAVTAAPG WQANEVLQMA ATVESASEHA VALAIAASTT 

       490        500        510        520        530        540 
HREPVANFRA VPGHGVSGTV AERAVRVGKP SWIASRCNST TLVTARRNAE LRGETAVFVE 

       550        560        570        580        590        600 
IDGEQCGVIA VADAVKASAA DAVAALHDRG FRTALLTGDN PASAAAVASR IGIDEVIADI 

       610        620        630        640        650        660 
LPEDKVDVIE QLRDRGHVVA MVGDGINDGP ALARADLGMA IGRGTDVAIG AADIILVRDN 

       670        680        690        700        710        720 
LDVVPITLDL AAATMRTIKF NMVWAFGYNI AAIPIAAAGL LNPLVAGAAM AFSSFFVVSN 

       730        740        750        760        770        780 
SLRLRNFGAI LSCGTSRHRT VKRWRCPPPT RLRSTACSPV DASPLRPVAH RTGVKPPTHR

« Hide

References

« Hide 'large scale' references
[1]"The Mycobacterium leprae genome: systematic sequence analysis identifies key catabolic enzymes, ATP-dependent transport systems and a novel polA locus associated with genomic variability."
Fsihi H., Cole S.T.
Mol. Microbiol. 16:909-919(1995) [PubMed: 7476188] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Massive gene decay in the leprosy bacillus."
Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. expand/collapse author list , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G.
Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z46257 Genomic DNA. Translation: CAA86358.1. Frameshift.
AL583924 Genomic DNA. Translation: CAC30942.1. Frameshift.
PIRF87157.
S77652.
RefSeqNP_302338.1. NC_002677.1.

3D structure databases

ProteinModelPortalP46839.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000029161; EBMYCP00000028767; EBMYCG00000029156.
GeneID909100.
GenomeReviewsGene locus ML1987 in contig AL450380_GR.
KEGGmle:ML1987.
PATRIC18057644. VBIMycLep78757_3746.

Organism-specific databases

LepromaML1987.
CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000016190.
HOGENOMHBG507745.
ProtClustDBCLSK790257.

Enzyme and pathway databases

BioCycMLEP272631:ML1987-MONOMER.

Family and domain databases

InterProIPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR006403. ATPase_P-typ_cat/Cu-transptr.
IPR000579. ATPase_P-typ_cation-transptr.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR006416. ATPase_P-typ_heavy-metal.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
IPR017969. Heavy-metal-associated_CS.
IPR006121. HeavyMe-assoc_HMA.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 1 hit.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:3.40.50.1000. HAD-like_dom. 2 hits.
KOK12949.
PfamPF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00940. CATPATPASEA.
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01511. ATPase-IB1_Cu. 1 hit.
TIGR01525. ATPase-IB_hvy. 1 hit.
TIGR01494. ATPase_P-type. 1 hit.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
PS01047. HMA_1. 1 hit.
PS50846. HMA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCTPA_MYCLE
AccessionPrimary (citable) accession number: P46839
Secondary accession number(s): Q9CBG9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 27, 2001
Last modified: January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents