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O34431 (ATCL_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-transporting ATPase
EC=3.6.3.8
Alternative name(s):
Calcium pump
Gene names
Name:yloB
Ordered Locus Names:BSU15650
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length890 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium. Ref.3

Catalytic activity

ATP + H2O + Ca2+[side 1] = ADP + phosphate + Ca2+[side 2].

Subcellular location

Cell membrane; Multi-pass membrane protein.

Developmental stage

Expressed from 4 hours and peaks at 9 hours after onset of sporulation. Ref.3

Disruption phenotype

Spores are less resistant to heat and germinate at a slower rate. Ref.3

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 890890Calcium-transporting ATPase
PRO_0000360851

Regions

Topological domain1 – 4747Cytoplasmic By similarity
Transmembrane48 – 6821Helical; Name=1; By similarity
Topological domain69 – 7810Extracellular By similarity
Transmembrane79 – 9921Helical; Name=2; By similarity
Topological domain100 – 238139Cytoplasmic By similarity
Transmembrane239 – 25820Helical; Name=3; By similarity
Topological domain259 – 27012Extracellular By similarity
Transmembrane271 – 28818Helical; Name=4; By similarity
Topological domain289 – 688400Cytoplasmic By similarity
Transmembrane689 – 70820Helical; Name=5; By similarity
Topological domain709 – 71810Extracellular By similarity
Transmembrane719 – 73921Helical; Name=6; By similarity
Topological domain740 – 75920Cytoplasmic By similarity
Transmembrane760 – 78223Helical; Name=7; By similarity
Topological domain783 – 79816Extracellular By similarity
Transmembrane799 – 81820Helical; Name=8; By similarity
Topological domain819 – 83012Cytoplasmic By similarity
Transmembrane831 – 84919Helical; Name=9; By similarity
Topological domain850 – 86415Extracellular By similarity
Transmembrane865 – 88521Helical; Name=10; By similarity
Topological domain886 – 8905Cytoplasmic By similarity

Sites

Active site32614-aspartylphosphate intermediate By similarity
Metal binding2791Calcium 2; via carbonyl oxygen By similarity
Metal binding2801Calcium 2; via carbonyl oxygen By similarity
Metal binding2821Calcium 2; via carbonyl oxygen By similarity
Metal binding2841Calcium 2 By similarity
Metal binding6331Magnesium By similarity
Metal binding6371Magnesium By similarity
Metal binding6991Calcium 1 By similarity
Metal binding7021Calcium 1 By similarity
Metal binding7271Calcium 2 By similarity
Metal binding7301Calcium 1 By similarity
Metal binding7311Calcium 1 By similarity
Metal binding7311Calcium 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O34431 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 43CB25F7A9BA31A6

FASTA89097,293
        10         20         30         40         50         60 
MKFHEMGQTD LLEATNTSMK QGLTEKEVKK RLDKHGPNEL QEGKKTSALL LFFAQFKDFM 

        70         80         90        100        110        120 
VLVLLAATLI SGFLGEYVDA VAIIAIVFVN GILGFFQERR AEQSLQALKE LSTPHVMALR 

       130        140        150        160        170        180 
EGSWTKIPSK ELVPGDIVKF TSGDRIGADV RIVEARSLEI EESALTGESI PVVKHADKLK 

       190        200        210        220        230        240 
KPDVSLGDIT NMAFMGTIVT RGSGVGVVVG TGMNTAMGKI ADMLESAGTL STPLQRRLEQ 

       250        260        270        280        290        300 
LGKILIVVAL LLTVLVVAVG VIQGHDLYSM FLAGVSLAVA AIPEGLPAIV TVALSLGVQR 

       310        320        330        340        350        360 
MIKQKSIVRK LPAVETLGCA SIICSDKTGT MTQNKMTVTH VWSGGKTWRV AGAGYEPKGS 

       370        380        390        400        410        420 
FTLNEKEISV NEHKPLQQML LFGALCNNSN IEKRDGEYVL DGDPTEGALL TAARKGGFSK 

       430        440        450        460        470        480 
EFVESNYRVI EEFPFDSARK MMTVIVENQD RKRYIITKGA PDVLMQRSSR IYYDGSAALF 

       490        500        510        520        530        540 
SNERKAETEA VLRHLASQAL RTIAVAYRPI KAGETPSMEQ AEKDLTMLGL SGIIDPPRPE 

       550        560        570        580        590        600 
VRQAIKECRE AGIKTVMITG DHVETAKAIA KDLRLLPKSG KIMDGKMLNE LSQEELSHVV 

       610        620        630        640        650        660 
EDVYVFARVS PEHKLKIVKA YQENGHIVAM TGDGVNDAPA IKQADIGVSM GITGTDVAKE 

       670        680        690        700        710        720 
ASSLVLVDDN FATIKSAIKE GRNIYENIRK FIRYLLASNV GEILVMLFAM LLALPLPLVP 

       730        740        750        760        770        780 
IQILWVNLVT DGLPAMALGM DQPEGDVMKR KPRHPKEGVF ARKLGWKVVS RGFLIGVATI 

       790        800        810        820        830        840 
LAFIIVYHRN PENLAYAQTI AFATLVLAQL IHVFDCRSET SVFSRNPFQN LYLIGAVLSS 

       850        860        870        880        890 
ILLMLVVIYY PPLQPIFHTV AITPGDWMLV IGMSAIPTFL LAGSLLTRKK

« Hide

References

« Hide 'large scale' references
[1]"A 28 kbp segment from the spoVM region of the Bacillus subtilis 168 genome."
Foulger D., Errington J.
Microbiology 144:801-805(1998) [PubMed: 9534248] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Expression of a P-type Ca(2+)-transport ATPase in Bacillus subtilis during sporulation."
Raeymaekers L., Wuytack E., Willems I., Michiels C.W., Wuytack F.
Cell Calcium 32:93-93(2002) [PubMed: 12161109] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
Strain: 168 / PS832.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y13937 Genomic DNA. Translation: CAA74269.1.
AL009126 Genomic DNA. Translation: CAB13439.1.
PIRH69877.
RefSeqNP_389448.1. NC_000964.3.

3D structure databases

HSSPHSSP built from PDB template 1WPG based on UniProtKB P04191.
ProteinModelPortalO34431.
SMRO34431. Positions 2-890.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001434; EBBACP00000001434; EBBACG00000001432.
GeneID936954.
GenomeReviewsGene locus BSU15650 in contig AL009126_GR.
KEGGbsu:BSU15650.
NMPDRfig|224308.1.peg.1567.
PATRIC18974937. VBIBacSub10457_1660.

Organism-specific databases

GenoListBSU15650.

Phylogenomic databases

GeneTreeEBGT00070000031890.
HOGENOMHBG456486.
OMALGEYIDA.
PhylomeDBO34431.
ProtClustDBCLSK873333.

Enzyme and pathway databases

BioCycBSUB:BSU15650-MONOMER.

Family and domain databases

InterProIPR023306. ATPase_cation_domN.
IPR008250. ATPase_P-typ_ATPase-assoc-dom.
IPR005782. ATPase_P-typ_Ca-transp.
IPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023300. ATPase_P-typ_cyto_domA.
IPR023299. ATPase_P-typ_cyto_domN.
IPR000695. ATPase_P-typ_H-transp.
IPR001757. ATPase_P-typ_ion-transptr.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
[Graphical view]
Gene3DG3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits.
G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit.
G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 2 hits.
KOK01537.
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF81660. ATPase_cation_domN. 1 hit.
SSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATCL_BACSU
AccessionPrimary (citable) accession number: O34431
Secondary accession number(s): Q799L2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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