P39621 (SPSA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spore coat polysaccharide biosynthesis protein spsA

Gene names

Name:	spsA
Ordered Locus Names:	BSU37910
ORF Names:	ipa-63d

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	256 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Glycosyltransferase implicated in the synthesis of the spore coat.
Pathway	Spore coat biogenesis; spore coat polysaccharide biosynthesis.
Subunit structure	Monomer in solution.
Domain	Contains an N-terminal nucleotide-binding domain and a C-terminal acceptor-binding domain.
Sequence similarities	Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	transferase activity, transferring glycosyl groups 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 – 256

256

Spore coat polysaccharide biosynthesis protein spsA

PRO_0000059219

Sites

Active site

191

1

Potential

Amino acid modifications

Disulfide bond

155 ↔ 243

Secondary structure

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256

Helix Strand Turn

Details...

Beta strand

4 – 12

9

Turn

14 – 16

3

Helix

17 – 25

9

Beta strand

32 – 38

7

Helix

43 – 49

7

Helix

50 – 54

5

Beta strand

58 – 62

5

Helix

68 – 73

6

Helix

76 – 87

12

Beta strand

91 – 97

7

Beta strand

100 – 102

3

Helix

106 – 116

11

Beta strand

122 – 132

11

Beta strand

138 – 144

7

Turn

154 – 156

3

Helix

159 – 161

3

Beta strand

162 – 165

4

Helix

166 – 176

11

Beta strand

177 – 180

4

Helix

184 – 189

6

Helix

190 – 198

9

Turn

199 – 201

3

Beta strand

204 – 216

13

Helix

234 – 236

3

Helix

243 – 251

9

Sequences

	Sequence		Length	Mass (Da)
	P39621 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: C20EA9627F5D536B	FASTA	256	30,184
	10 20 30 40 50 60 MPKVSVIMTS YNKSDYVAKS ISSILSQTFS DFELFIMDDN SNEETLNVIR PFLNDNRVRF 70 80 90 100 110 120 YQSDISGVKE RTEKTRYAAL INQAIEMAEG EYITYATDDN IYMPDRLLKM VRELDTHPEK 130 140 150 160 170 180 AVIYSASKTY HLNENRDIVK ETVRPAAQVT WNAPCAIDHC SVMHRYSVLE KVKEKFGSYW 190 200 210 220 230 240 DESPAFYRIG DARFFWRVNH FYPFYPLDEE LDLNYITDQS IHFQLFELEK NEFVRNLPPQ 250 RNCRELRESL KKLGMG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325 degrees to 333 degrees." Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E., Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A. Mol. Microbiol. 10:371-384(1993) [PubMed: 7934828] [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. , 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]	"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: 10089467] [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: 10350455] [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: 11733986] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X73124 Genomic DNA. Translation: CAA51619.1.
AL009126 Genomic DNA. Translation: CAB15817.1.

PIR

S39718.

RefSeq

NP_391670.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H7L	X-ray	1.98	A	2-256	[»]
1H7Q	X-ray	2.00	A	2-256	[»]
1QG8	X-ray	1.50	A	2-256	[»]
1QGQ	X-ray	1.50	A	2-256	[»]
1QGS	X-ray	2.00	A	2-256	[»]

ProteinModelPortal

P39621.

SMR

P39621. Positions 2-256.

ModBase

Search...

Protein family/group databases

CAZy

GT2. Glycosyltransferase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000000453; EBBACP00000000453; EBBACG00000000451.

GeneID

937253.

GenomeReviews

Gene locus BSU37910 in contig AL009126_GR.

KEGG

bsu:BSU37910.

NMPDR

fig|224308.1.peg.3796.

PATRIC

18979622. VBIBacSub10457_3973.

Organism-specific databases

GenoList

BSU37910. [Micado]

Phylogenomic databases

GeneTree

EBGT00070000032319.

HOGENOM

HBG338447.

OMA

DFELFIM.

PhylomeDB

P39621.

ProtClustDB

CLSK873590.

Enzyme and pathway databases

BioCyc

BSUB:BSU37910-MONOMER.

Family and domain databases

InterPro

IPR001173. Glyco_trans_2.
[Graphical view]

Pfam

PF00535. Glycos_transf_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SPSA_BACSU

Accession

Primary (citable) accession number: P39621

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program