SRTD_BACSU
ID SRTD_BACSU Reviewed; 198 AA.
AC P54603;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Sortase D {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
GN Name=srtD {ECO:0000303|PubMed:21906378};
GN Synonyms=srtA {ECO:0000312|EMBL:CAB12748.1}, yhcS;
GN OrderedLocusNames=BSU09200;
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=8969498; DOI=10.1099/13500872-142-11-3021;
RA Noback M.A., Terpstra P., Holsappel S., Venema G., Bron S.;
RT "A 22 kb DNA sequence in the cspB-glpPFKD region at 75 degrees on the
RT Bacillus subtilis chromosome.";
RL Microbiology 142:3021-3026(1996).
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 FUNCTION AS A SORTASE, AND INDUCTION.
RX PubMed=21906378; DOI=10.1186/2191-0855-1-22;
RA Nguyen H.D., Phan T.T., Schumann W.;
RT "Analysis and application of Bacillus subtilis sortases to anchor
RT recombinant proteins on the cell wall.";
RL AMB Express 1:22-22(2011).
RN [4]
RP FUNCTION AS A SORTASE, AND DISRUPTION PHENOTYPE.
RX PubMed=21800427; DOI=10.1002/pmic.201100174;
RA Fasehee H., Westers H., Bolhuis A., Antelmann H., Hecker M., Quax W.J.,
RA Mirlohi A.F., van Dijl J.M., Ahmadian G.;
RT "Functional analysis of the sortase YhcS in Bacillus subtilis.";
RL Proteomics 11:3905-3913(2011).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22020651; DOI=10.1128/jb.05711-11;
RA Liew P.X., Wang C.L., Wong S.L.;
RT "Functional characterization and localization of a Bacillus subtilis
RT sortase and its substrate and use of this sortase system to covalently
RT anchor a heterologous protein to the B. subtilis cell wall for surface
RT display.";
RL J. Bacteriol. 194:161-175(2012).
CC -!- FUNCTION: Transpeptidase that anchors surface proteins to the cell wall
CC (PubMed:21906378, PubMed:21800427, PubMed:22020651). Recognizes and
CC modifies its substrate by proteolytic cleavage of a C-terminal sorting
CC signal. Following cleavage, a covalent intermediate is formed via a
CC thioester bond between the sortase and its substrate, which is then
CC transferred and covalently attached to the cell wall (Probable). This
CC sortase recognizes a Leu-Pro-Asp-Thr-Ser/Ala (LPDTS/A) motif
CC (PubMed:21906378, PubMed:22020651). It has two substrates, YhcR and
CC YfkN (PubMed:21906378, PubMed:21800427, PubMed:22020651).
CC {ECO:0000269|PubMed:21800427, ECO:0000269|PubMed:21906378,
CC ECO:0000269|PubMed:22020651, ECO:0000305|PubMed:21800427,
CC ECO:0000305|PubMed:21906378, ECO:0000305|PubMed:22020651}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22020651};
CC Single-pass type II membrane protein {ECO:0000305}. Note=Nonuniformly
CC distributed around the cell periphery in the form of patches or short
CC arcs. {ECO:0000269|PubMed:22020651}.
CC -!- INDUCTION: Preferentially expressed in the late stationary phase.
CC {ECO:0000269|PubMed:21906378}.
CC -!- DISRUPTION PHENOTYPE: Mutant releases elevated levels of the sortase
CC substrate YfkN into the culture medium upon phosphate starvation
CC (PubMed:21800427). Inactivation of the gene abolishes the cell wall
CC anchoring of a fusion protein composed of a beta-lactamase reporter and
CC the C-terminal region of the sortase substrate YhcR (PubMed:22020651).
CC {ECO:0000269|PubMed:21800427, ECO:0000269|PubMed:22020651}.
CC -!- SIMILARITY: Belongs to the bacterial sortase family. Class D subfamily.
CC {ECO:0000305}.
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DR EMBL; X96983; CAA65703.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12748.1; -; Genomic_DNA.
DR PIR; G69823; G69823.
DR RefSeq; NP_388801.1; NC_000964.3.
DR RefSeq; WP_003244666.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P54603; -.
DR SMR; P54603; -.
DR STRING; 224308.BSU09200; -.
DR MEROPS; C60.008; -.
DR PaxDb; P54603; -.
DR PRIDE; P54603; -.
DR EnsemblBacteria; CAB12748; CAB12748; BSU_09200.
DR GeneID; 939748; -.
DR KEGG; bsu:BSU09200; -.
DR PATRIC; fig|224308.179.peg.992; -.
DR eggNOG; COG3764; Bacteria.
DR InParanoid; P54603; -.
DR OMA; IYGKRVT; -.
DR PhylomeDB; P54603; -.
DR BioCyc; BSUB:BSU09200-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05828; Sortase_D_1; 1.
DR Gene3D; 2.40.260.10; -; 1.
DR InterPro; IPR005754; Sortase.
DR InterPro; IPR041999; Sortase_D_1.
DR InterPro; IPR023365; Sortase_dom-sf.
DR Pfam; PF04203; Sortase; 1.
DR SUPFAM; SSF63817; SSF63817; 1.
DR TIGRFAMs; TIGR01076; sortase_fam; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Thiol protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..198
FT /note="Sortase D"
FT /id="PRO_0000049566"
FT TRANSMEM 7..25
FT /note="Helical; Note=Membrane anchor"
FT /evidence="ECO:0000255, ECO:0000305"
FT REGION 36..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q2FV99"
FT ACT_SITE 177
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q2FV99"
FT SITE 189
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q2FV99"
SQ SEQUENCE 198 AA; 21976 MW; 286C6F96CAA96A43 CRC64;
MKKVIPLFII AAGLVIAGYG GFKLIDTNTK TEQTLKEAKL AAKKPQEASG TKNSTDQAKN
KASFKPETGQ ASGILEIPKI NAELPIVEGT DADDLEKGVG HYKDSYYPDE NGQIVLSGHR
DTVFRRTGEL EKGDQLRLLL SYGEFTYEIV KTKIVDKDDT SIITLQHEKE ELILTTCYPF
SYVGNAPKRY IIYGKRVT
