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Protein

Spore coat polysaccharide biosynthesis protein SpsA

Gene

spsA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Glycosyltransferase implicated in the synthesis of the spore coat.

Pathwayi: spore coat polysaccharide biosynthesis

This protein is involved in the pathway spore coat polysaccharide biosynthesis, which is part of Spore coat biogenesis.
View all proteins of this organism that are known to be involved in the pathway spore coat polysaccharide biosynthesis and in Spore coat biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei191 – 1911Sequence analysis

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciBSUB:BSU37910-MONOMER.
UniPathwayiUPA00953.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Spore coat polysaccharide biosynthesis protein SpsA
Gene namesi
Name:spsA
Ordered Locus Names:BSU37910
ORF Names:ipa-63d
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 256256Spore coat polysaccharide biosynthesis protein SpsAPRO_0000059219Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi155 ↔ 243

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP39621.

Interactioni

Subunit structurei

Monomer in solution.

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100020471.

Structurei

Secondary structure

1
256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 129Combined sources
Turni14 – 163Combined sources
Helixi17 – 259Combined sources
Beta strandi32 – 387Combined sources
Helixi43 – 497Combined sources
Helixi50 – 545Combined sources
Beta strandi58 – 625Combined sources
Helixi68 – 725Combined sources
Helixi76 – 8712Combined sources
Beta strandi91 – 977Combined sources
Beta strandi100 – 1023Combined sources
Helixi106 – 11611Combined sources
Beta strandi122 – 13211Combined sources
Beta strandi138 – 1447Combined sources
Turni154 – 1563Combined sources
Helixi159 – 1613Combined sources
Beta strandi162 – 1654Combined sources
Helixi167 – 17610Combined sources
Beta strandi177 – 1804Combined sources
Helixi184 – 1863Combined sources
Helixi190 – 1989Combined sources
Turni199 – 2013Combined sources
Beta strandi204 – 21613Combined sources
Helixi234 – 2363Combined sources
Helixi243 – 25311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H7LX-ray1.98A2-256[»]
1H7QX-ray2.00A2-256[»]
1QG8X-ray1.50A2-256[»]
1QGQX-ray1.50A2-256[»]
1QGSX-ray2.00A2-256[»]
ProteinModelPortaliP39621.
SMRiP39621. Positions 2-256.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39621.

Family & Domainsi

Domaini

Contains an N-terminal nucleotide-binding domain and a C-terminal acceptor-binding domain.

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Phylogenomic databases

eggNOGiCOG0463. LUCA.
HOGENOMiHOG000009198.
InParanoidiP39621.
OMAiDFELFIM.
OrthoDBiEOG6M0T47.
PhylomeDBiP39621.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

P39621-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKVSVIMTS YNKSDYVAKS ISSILSQTFS DFELFIMDDN SNEETLNVIR
60 70 80 90 100
PFLNDNRVRF YQSDISGVKE RTEKTRYAAL INQAIEMAEG EYITYATDDN
110 120 130 140 150
IYMPDRLLKM VRELDTHPEK AVIYSASKTY HLNENRDIVK ETVRPAAQVT
160 170 180 190 200
WNAPCAIDHC SVMHRYSVLE KVKEKFGSYW DESPAFYRIG DARFFWRVNH
210 220 230 240 250
FYPFYPLDEE LDLNYITDQS IHFQLFELEK NEFVRNLPPQ RNCRELRESL

KKLGMG
Length:256
Mass (Da):30,184
Last modified:February 1, 1995 - v1
Checksum:iC20EA9627F5D536B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73124 Genomic DNA. Translation: CAA51619.1.
AL009126 Genomic DNA. Translation: CAB15817.1.
PIRiS39718.
RefSeqiNP_391670.1. NC_000964.3.
WP_003244383.1. NZ_JNCM01000034.1.

Genome annotation databases

EnsemblBacteriaiCAB15817; CAB15817; BSU37910.
GeneIDi937253.
KEGGibsu:BSU37910.
PATRICi18979622. VBIBacSub10457_3973.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X73124 Genomic DNA. Translation: CAA51619.1.
AL009126 Genomic DNA. Translation: CAB15817.1.
PIRiS39718.
RefSeqiNP_391670.1. NC_000964.3.
WP_003244383.1. NZ_JNCM01000034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H7LX-ray1.98A2-256[»]
1H7QX-ray2.00A2-256[»]
1QG8X-ray1.50A2-256[»]
1QGQX-ray1.50A2-256[»]
1QGSX-ray2.00A2-256[»]
ProteinModelPortaliP39621.
SMRiP39621. Positions 2-256.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100020471.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Proteomic databases

PaxDbiP39621.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15817; CAB15817; BSU37910.
GeneIDi937253.
KEGGibsu:BSU37910.
PATRICi18979622. VBIBacSub10457_3973.

Phylogenomic databases

eggNOGiCOG0463. LUCA.
HOGENOMiHOG000009198.
InParanoidiP39621.
OMAiDFELFIM.
OrthoDBiEOG6M0T47.
PhylomeDBiP39621.

Enzyme and pathway databases

UniPathwayiUPA00953.
BioCyciBSUB:BSU37910-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP39621.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Cloning, crystallization and preliminary X-ray analysis of a nucleotide-diphospho-sugar transferase spsA from Bacillus subtilis."
    Charnock S.J., Davies G.J.
    Acta Crystallogr. D 55:677-678(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  4. "Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms."
    Charnock S.J., Davies G.J.
    Biochemistry 38:6380-6385(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
  5. "Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: a comparison with related NDP-sugar glycosyltransferases."
    Tarbouriech N., Charnock S.J., Davies G.J.
    J. Mol. Biol. 314:655-661(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS).

Entry informationi

Entry nameiSPSA_BACSU
AccessioniPrimary (citable) accession number: P39621
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 17, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.