SPSA_BACSU
ID SPSA_BACSU Reviewed; 256 AA.
AC P39621;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Spore coat polysaccharide biosynthesis protein SpsA;
GN Name=spsA; OrderedLocusNames=BSU37910; ORFNames=ipa-63d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=10089467; DOI=10.1107/s0907444998013006;
RA Charnock S.J., Davies G.J.;
RT "Cloning, crystallization and preliminary X-ray analysis of a nucleotide-
RT diphospho-sugar transferase spsA from Bacillus subtilis.";
RL Acta Crystallogr. D 55:677-678(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=10350455; DOI=10.1021/bi990270y;
RA Charnock S.J., Davies G.J.;
RT "Structure of the nucleotide-diphospho-sugar transferase, SpsA from
RT Bacillus subtilis, in native and nucleotide-complexed forms.";
RL Biochemistry 38:6380-6385(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS).
RX PubMed=11733986; DOI=10.1006/jmbi.2001.5159;
RA Tarbouriech N., Charnock S.J., Davies G.J.;
RT "Three-dimensional structures of the Mn and Mg dTDP complexes of the family
RT GT-2 glycosyltransferase SpsA: a comparison with related NDP-sugar
RT glycosyltransferases.";
RL J. Mol. Biol. 314:655-661(2001).
CC -!- FUNCTION: Glycosyltransferase implicated in the synthesis of the spore
CC coat.
CC -!- PATHWAY: Spore coat biogenesis; spore coat polysaccharide biosynthesis.
CC -!- SUBUNIT: Monomer in solution.
CC -!- DOMAIN: Contains an N-terminal nucleotide-binding domain and a C-
CC terminal acceptor-binding domain.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; X73124; CAA51619.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15817.1; -; Genomic_DNA.
DR PIR; S39718; S39718.
DR RefSeq; NP_391670.1; NC_000964.3.
DR RefSeq; WP_003244383.1; NZ_JNCM01000034.1.
DR PDB; 1H7L; X-ray; 1.98 A; A=2-256.
DR PDB; 1H7Q; X-ray; 2.00 A; A=2-256.
DR PDB; 1QG8; X-ray; 1.50 A; A=2-256.
DR PDB; 1QGQ; X-ray; 1.50 A; A=2-256.
DR PDB; 1QGS; X-ray; 2.00 A; A=2-256.
DR PDBsum; 1H7L; -.
DR PDBsum; 1H7Q; -.
DR PDBsum; 1QG8; -.
DR PDBsum; 1QGQ; -.
DR PDBsum; 1QGS; -.
DR AlphaFoldDB; P39621; -.
DR SMR; P39621; -.
DR STRING; 224308.BSU37910; -.
DR DrugBank; DB03435; Uridine-5'-Diphosphate.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; P39621; -.
DR PRIDE; P39621; -.
DR EnsemblBacteria; CAB15817; CAB15817; BSU_37910.
DR GeneID; 937253; -.
DR KEGG; bsu:BSU37910; -.
DR PATRIC; fig|224308.179.peg.4104; -.
DR eggNOG; COG0463; Bacteria.
DR InParanoid; P39621; -.
DR OMA; DFELFIM; -.
DR PhylomeDB; P39621; -.
DR BioCyc; BSUB:BSU37910-MON; -.
DR UniPathway; UPA00953; -.
DR EvolutionaryTrace; P39621; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..256
FT /note="Spore coat polysaccharide biosynthesis protein SpsA"
FT /id="PRO_0000059219"
FT ACT_SITE 191
FT /evidence="ECO:0000255"
FT DISULFID 155..243
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:1QG8"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:1QG8"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:1QG8"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1QG8"
FT HELIX 43..49
FT /evidence="ECO:0007829|PDB:1QG8"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:1QG8"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1QG8"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:1QG8"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:1QG8"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1QG8"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1QG8"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:1QG8"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:1QG8"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:1QG8"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:1QG8"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1QG8"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1QG8"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:1QG8"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:1QG8"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1QG8"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:1QG8"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:1QG8"
FT STRAND 204..216
FT /evidence="ECO:0007829|PDB:1QG8"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1QG8"
FT HELIX 243..253
FT /evidence="ECO:0007829|PDB:1QG8"
SQ SEQUENCE 256 AA; 30184 MW; C20EA9627F5D536B CRC64;
MPKVSVIMTS YNKSDYVAKS ISSILSQTFS DFELFIMDDN SNEETLNVIR PFLNDNRVRF
YQSDISGVKE RTEKTRYAAL INQAIEMAEG EYITYATDDN IYMPDRLLKM VRELDTHPEK
AVIYSASKTY HLNENRDIVK ETVRPAAQVT WNAPCAIDHC SVMHRYSVLE KVKEKFGSYW
DESPAFYRIG DARFFWRVNH FYPFYPLDEE LDLNYITDQS IHFQLFELEK NEFVRNLPPQ
RNCRELRESL KKLGMG
