Q10877 (CTPB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cation-transporting P-type ATPase B
EC=3.6.3.-

Gene names

Name:	ctpB
Ordered Locus Names:	Rv0103c, MT0112
ORF Names:	MTCY251.22c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	752 AA.
Sequence status	Complete.
Protein existence	Inferred 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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from direct assay. Source: MTBBASE integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 752	752	Cation-transporting P-type ATPase B		PRO_0000046168
Regions
	Transmembrane	105 – 125	21	Helical; Potential
	Transmembrane	132 – 152	21	Helical; Potential
	Transmembrane	167 – 187	21	Helical; Potential
	Transmembrane	201 – 221	21	Helical; Potential
	Transmembrane	361 – 381	21	Helical; Potential
	Transmembrane	390 – 410	21	Helical; Potential
	Transmembrane	491 – 511	21	Helical; Potential
	Transmembrane	714 – 734	21	Helical; Potential
	Domain	16 – 79	64	HMA
Sites
	Active site	446	1	4-aspartylphosphate intermediate By similarity
	Metal binding	26	1	By similarity
	Metal binding	29	1	By similarity
Experimental info
	Sequence conflict	22	1	L → S in AAK44334. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q10877 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 21563FE4B4407505	FASTA	752	77,509
	10 20 30 40 50 60 MAAPVVGDAD LQSVRRIRLD VLGMSCAACA SRVETKLNKI PGVRASVNFA TRVATIDAVG 70 80 90 100 110 120 MAADELCGVV EKAGYHAAPH TETTVLDKRT KDPDGAHARR LLRRLLVAAV LFVPLADLST 130 140 150 160 170 180 LFAIVPSARV PGWGYILTAL AAPVVTWAAW PFHSVALRNA RHRTTSMETL ISVGIVAATA 190 200 210 220 230 240 WSLSSVFGDQ PPREGSGIWR AILNSDSIYL EVAAGVTVFV LAGRYFEARA KSKAGSALRA 250 260 270 280 290 300 LAELGAKNVA VLLPDGAELV IPASELKKRQ RFVTRPGETI AADGVVVDGS AAIDMSAMTG 310 320 330 340 350 360 EAKPVRAYPA ASVVGGTVVM DGRLVIEATA VGADTQFAAM VRLVEQAQTQ KARAQRLADH 370 380 390 400 410 420 IAGVFVPVVF VIAGLAGAAW LVSGAGADRA FSVTLGVLVI ACPCALGLAT PTAMMVASGR 430 440 450 460 470 480 GAQLGIFIKG YRALETIRSI DTVVFDKTGT LTVGQLAVST VTMAGSGTSE RDREEVLGLA 490 500 510 520 530 540 AAVESASEHA MAAAIVAASP DPGPVNGFVA VAGCGVSGEV GGHHVEVGKP SWITRTTPCH 550 560 570 580 590 600 DAALVSARLD GESRGETVVF VSVDGVVRAA LTIADTLKDS AAAAVAALRS RGLRTILLTG 610 620 630 640 650 660 DNRAAADAVA AQVGIDSAVA DMLPEGKVDV IQRLREEGHT VAMVGDGIND GPALVGADLG 670 680 690 700 710 720 LAIGRGTDVA LGAADIILVR DDLNTVPQAL DLARATMRTI RMNMIWAFGY NVAAIPIAAA 730 740 750 GLLNPLIAGA AMAFSSFFVV SNSLRLRNFG AQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Agranoff D.D., Krishna S.K., Griffin G.E., Mangan J. Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[3]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y07638 Genomic DNA. Translation: CAA68915.1. BX842572 Genomic DNA. Translation: CAA98939.1. AE000516 Genomic DNA. Translation: AAK44334.1.
PIR	G70751.
RefSeq	NP_214617.1. NC_000962.2. NP_334520.1. NC_002755.2.
3D structure databases
ProteinModelPortal	Q10877.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000003428; EBMYCP00000003428; EBMYCG00000003426. EBMYCT00000072297; EBMYCP00000070356; EBMYCG00000072292.
GeneID	886928. 922962.
GenomeReviews	Gene locus MT0112 in contig AE000516_GR. Gene locus Rv0103c in contig AL123456_GR.
KEGG	mtc:MT0112. mtu:Rv0103c.
PATRIC	18121970. VBIMycTub22151_0119.
TIGR	MT0112.
Organism-specific databases
TubercuList	Rv0103c.
Phylogenomic databases
GeneTree	EBGT00050000016190.
HOGENOM	HBG507745.
OMA	HAESQGH.
PhylomeDB	Q10877.
ProtClustDB	CLSK790257.
Family and domain databases
InterPro	IPR008250. 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]
Gene3D	G3DSA: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.
KO	K12949.
Pfam	PF00122. E1-E2_ATPase. 1 hit. PF00403. HMA. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00940. CATPATPASEA.
SUPFAM	SSF56784. HAD-like_dom. 1 hit. SSF55008. HeavyMe_transpt. 1 hit.
TIGRFAMs	TIGR01511. ATPase-IB1_Cu. 1 hit. TIGR01525. ATPase-IB_hvy. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. PS01047. HMA_1. 1 hit. PS50846. HMA_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CTPB_MYCTU

Accession

Primary (citable) accession number: Q10877
Secondary accession number(s): P77905

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program