SRTA_STAA8
ID SRTA_STAA8 Reviewed; 206 AA.
AC Q2FV99;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Sortase A {ECO:0000305};
DE EC=3.4.22.70 {ECO:0000269|PubMed:10535938, ECO:0000269|PubMed:11371637, ECO:0000269|PubMed:14503881, ECO:0000269|PubMed:14769030, ECO:0000269|PubMed:15247224, ECO:0000269|PubMed:16269411, ECO:0000269|PubMed:17518446};
DE AltName: Full=Surface protein sorting A {ECO:0000303|PubMed:10427003};
GN Name=srtA {ECO:0000303|PubMed:10427003};
GN OrderedLocusNames=SAOUHSC_02834 {ECO:0000312|EMBL:ABD31836.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10427003; DOI=10.1126/science.285.5428.760;
RA Mazmanian S.K., Liu G., Ton-That H., Schneewind O.;
RT "Staphylococcus aureus sortase, an enzyme that anchors surface proteins to
RT the cell wall.";
RL Science 285:760-763(1999).
RN [3]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=10446208; DOI=10.1074/jbc.274.34.24316;
RA Ton-That H., Schneewind O.;
RT "Anchor structure of staphylococcal surface proteins. IV. Inhibitors of the
RT cell wall sorting reaction.";
RL J. Biol. Chem. 274:24316-24320(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP CYS-184.
RC STRAIN=BB270, and RN4220 / OS2;
RX PubMed=10535938; DOI=10.1073/pnas.96.22.12424;
RA Ton-That H., Liu G., Mazmanian S.K., Faull K.F., Schneewind O.;
RT "Purification and characterization of sortase, the transpeptidase that
RT cleaves surface proteins of Staphylococcus aureus at the LPXTG motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12424-12429(1999).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10805806; DOI=10.1073/pnas.080520697;
RA Mazmanian S.K., Liu G., Jensen E.R., Lenoy E., Schneewind O.;
RT "Staphylococcus aureus sortase mutants defective in the display of surface
RT proteins and in the pathogenesis of animal infections.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5510-5515(2000).
RN [6]
RP FUNCTION, MUTAGENESIS OF HIS-120; CYS-184 AND TRP-194, AND ACTIVE SITE.
RX PubMed=11714722; DOI=10.1074/jbc.m109945200;
RA Ton-That H., Mazmanian S.K., Alksne L., Schneewind O.;
RT "Anchoring of surface proteins to the cell wall of Staphylococcus aureus.
RT Cysteine 184 and histidine 120 of sortase form a thiolate-imidazolium ion
RT pair for catalysis.";
RL J. Biol. Chem. 277:7447-7452(2002).
RN [7]
RP FUNCTION.
RX PubMed=11856734; DOI=10.1074/jbc.m109194200;
RA Perry A.M., Ton-That H., Mazmanian S.K., Schneewind O.;
RT "Anchoring of surface proteins to the cell wall of Staphylococcus aureus.
RT III. Lipid II is an in vivo peptidoglycan substrate for sortase-catalyzed
RT surface protein anchoring.";
RL J. Biol. Chem. 277:16241-16248(2002).
RN [8]
RP CATALYTIC ACTIVITY.
RX PubMed=14503881; DOI=10.1021/bi034391g;
RA Huang X., Aulabaugh A., Ding W., Kapoor B., Alksne L., Tabei K.,
RA Ellestad G.;
RT "Kinetic mechanism of Staphylococcus aureus sortase SrtA.";
RL Biochemistry 42:11307-11315(2003).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RX PubMed=14769030; DOI=10.1021/bi035920j;
RA Kruger R.G., Otvos B., Frankel B.A., Bentley M., Dostal P.,
RA McCafferty D.G.;
RT "Analysis of the substrate specificity of the Staphylococcus aureus sortase
RT transpeptidase SrtA.";
RL Biochemistry 43:1541-1551(2004).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASN-98; CYS-184 AND ARG-197,
RP AND ACTIVE SITE.
RX PubMed=15247224; DOI=10.1074/jbc.m405282200;
RA Marraffini L.A., Ton-That H., Zong Y., Narayana S.V., Schneewind O.;
RT "Anchoring of surface proteins to the cell wall of Staphylococcus aureus. A
RT conserved arginine residue is required for efficient catalysis of sortase
RT A.";
RL J. Biol. Chem. 279:37763-37770(2004).
RN [11]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, CALCIUM-BINDING, AND MUTAGENESIS
RP OF GLU-108; ASP-170 AND GLU-171.
RX PubMed=16269411; DOI=10.1074/jbc.m506123200;
RA Naik M.T., Suree N., Ilangovan U., Liew C.K., Thieu W., Campbell D.O.,
RA Clemens J.J., Jung M.E., Clubb R.T.;
RT "Staphylococcus aureus sortase A transpeptidase. Calcium promotes sorting
RT signal binding by altering the mobility and structure of an active site
RT loop.";
RL J. Biol. Chem. 281:1817-1826(2006).
RN [12]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-120; THR-180; LEU-181; ILE-182;
RP THR-183; CYS-184; ASP-185; ASP-186 AND ARG-197, AND ACTIVE SITE.
RX PubMed=17518446; DOI=10.1021/bi700448e;
RA Frankel B.A., Tong Y., Bentley M.L., Fitzgerald M.C., McCafferty D.G.;
RT "Mutational analysis of active site residues in the Staphylococcus aureus
RT transpeptidase SrtA.";
RL Biochemistry 46:7269-7278(2007).
RN [13]
RP SUBUNIT.
RX PubMed=17658894; DOI=10.1021/bi700519w;
RA Lu C., Zhu J., Wang Y., Umeda A., Cowmeadow R.B., Lai E., Moreno G.N.,
RA Person M.D., Zhang Z.;
RT "Staphylococcus aureus sortase A exists as a dimeric protein in vitro.";
RL Biochemistry 46:9346-9354(2007).
RN [14]
RP ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND MUTAGENESIS OF ASN-132; LYS-137 AND TYR-143.
RC STRAIN=RN4220;
RX PubMed=26129884; DOI=10.1177/1535370215592122;
RA Zhu J., Xiang L., Jiang F., Zhang Z.J.;
RT "Equilibrium of sortase A dimerization on Staphylococcus aureus cell
RT surface mediates its cell wall sorting activity.";
RL Exp. Biol. Med. (Maywood) 241:90-100(2016).
RN [15] {ECO:0007744|PDB:1IJA}
RP STRUCTURE BY NMR OF 59-206, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, AND ACTIVE SITE.
RC STRAIN=RN4220 / OS2;
RX PubMed=11371637; DOI=10.1073/pnas.101064198;
RA Ilangovan U., Ton-That H., Iwahara J., Schneewind O., Clubb R.T.;
RT "Structure of sortase, the transpeptidase that anchors proteins to the cell
RT wall of Staphylococcus aureus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:6056-6061(2001).
RN [16] {ECO:0007744|PDB:1T2O, ECO:0007744|PDB:1T2P, ECO:0007744|PDB:1T2W}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 62-206 OF WILD-TYPE; MUTANT
RP ALA-184 AND MUTANT ALA-184 IN COMPLEX WITH A LPETG PEPTIDE, AND ACTIVE
RP SITE.
RX PubMed=15117963; DOI=10.1074/jbc.m401374200;
RA Zong Y., Bice T.W., Ton-That H., Schneewind O., Narayana S.V.;
RT "Crystal structures of Staphylococcus aureus sortase A and its substrate
RT complex.";
RL J. Biol. Chem. 279:31383-31389(2004).
RN [17] {ECO:0007744|PDB:2KID}
RP STRUCTURE BY NMR OF 59-206 IN COMPLEX WITH SUBSTRATE ANALOG AND CALCIUM,
RP AND MUTAGENESIS OF LEU-97; ALA-104 AND ALA-118.
RX PubMed=19592495; DOI=10.1074/jbc.m109.022624;
RA Suree N., Liew C.K., Villareal V.A., Thieu W., Fadeev E.A., Clemens J.J.,
RA Jung M.E., Clubb R.T.;
RT "The structure of the Staphylococcus aureus sortase-substrate complex
RT reveals how the universally conserved LPXTG sorting signal is recognized.";
RL J. Biol. Chem. 284:24465-24477(2009).
CC -!- FUNCTION: Transpeptidase that anchors surface proteins to the cell wall
CC (PubMed:10427003, PubMed:10446208, PubMed:10535938, PubMed:11714722,
CC PubMed:14769030, PubMed:15247224). Recognizes and modifies its
CC substrate by proteolytic cleavage of a C-terminal sorting signal.
CC Following cleavage, a covalent intermediate is formed via a thioester
CC bond between the sortase and its substrate, which is then transferred
CC and covalently attached to the cell wall (PubMed:10446208,
CC PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224).
CC This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is
CC cleaved by the sortase between the threonine and glycine residues
CC (PubMed:10535938, PubMed:11714722, PubMed:14769030, PubMed:15247224).
CC Utilizes lipid II as the peptidoglycan substrate for the sorting
CC reaction (PubMed:10446208, PubMed:11856734). Responsible for the
CC display of important virulence factors (PubMed:14769030). Important for
CC interactions with the host and host colonization during infection
CC (PubMed:10805806, PubMed:14769030). {ECO:0000269|PubMed:10427003,
CC ECO:0000269|PubMed:10446208, ECO:0000269|PubMed:10535938,
CC ECO:0000269|PubMed:10805806, ECO:0000269|PubMed:11714722,
CC ECO:0000269|PubMed:11856734, ECO:0000269|PubMed:14769030,
CC ECO:0000269|PubMed:15247224}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The enzyme catalyzes a cell wall sorting reaction in which a
CC surface protein with a sorting signal containing a LPXTG motif is
CC cleaved between the Thr and Gly residue. The resulting threonine
CC carboxyl end of the protein is covalently attached to a pentaglycine
CC cross-bridge of peptidoglycan.; EC=3.4.22.70;
CC Evidence={ECO:0000269|PubMed:10535938, ECO:0000269|PubMed:11371637,
CC ECO:0000269|PubMed:14503881, ECO:0000269|PubMed:14769030,
CC ECO:0000269|PubMed:15247224, ECO:0000269|PubMed:16269411,
CC ECO:0000269|PubMed:17518446};
CC -!- ACTIVITY REGULATION: Sortase activity is regulated by monomer-homodimer
CC equilibrium. Mutant cells with monomeric SrtA display more adhesive
CC proteins on the cell surface and are more invasive than wild-type
CC cells, which have majority of SrtA in dimeric form. Dimerization may
CC suppress the enzymatic activity on cell membranes (PubMed:26129884).
CC Stimulated by calcium ions, which promote substrate binding
CC (PubMed:11371637, PubMed:16269411). Calcium ions bind to SrtA and
CC modulate both the structure and dynamics of a large active site loop
CC (PubMed:16269411). Can also be stimulated, to a lesser extent, by
CC Mg(2+) and Mn(2+) (PubMed:11371637). Inhibited by sulfhydryl-modifying
CC reagents (PubMed:10535938, PubMed:10446208).
CC {ECO:0000269|PubMed:10446208, ECO:0000269|PubMed:10535938,
CC ECO:0000269|PubMed:11371637, ECO:0000269|PubMed:16269411,
CC ECO:0000269|PubMed:26129884}.
CC -!- SUBUNIT: Monomer and homodimer; in equilibrium.
CC {ECO:0000269|PubMed:17658894, ECO:0000269|PubMed:26129884}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26129884,
CC ECO:0000305|PubMed:11371637}; Single-pass type II membrane protein
CC {ECO:0000305|PubMed:11371637}.
CC -!- DISRUPTION PHENOTYPE: Mutants fail to cleave and anchor surface
CC proteins (PubMed:10427003, PubMed:10805806). Protein secretion pathway
CC is not affected (PubMed:10805806). Mutants are defective in the
CC establishment of animal infections (PubMed:10805806).
CC {ECO:0000269|PubMed:10427003, ECO:0000269|PubMed:10805806}.
CC -!- BIOTECHNOLOGY: Could be used as a target for the development of
CC antivirulence chemotherapeutics against Gram-positive bacterial
CC pathogens. {ECO:0000305|PubMed:14769030}.
CC -!- SIMILARITY: Belongs to the bacterial sortase family. Class A subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000253; ABD31836.1; -; Genomic_DNA.
DR RefSeq; WP_000759361.1; NZ_LS483365.1.
DR RefSeq; YP_501293.1; NC_007795.1.
DR PDB; 1IJA; NMR; -; A=59-206.
DR PDB; 1T2O; X-ray; 2.30 A; A/B/C=61-206.
DR PDB; 1T2P; X-ray; 2.00 A; A/B/C=61-206.
DR PDB; 1T2W; X-ray; 1.80 A; A/B/C=62-206.
DR PDB; 2KID; NMR; -; A=59-206.
DR PDB; 6R1V; NMR; -; A=59-206.
DR PDB; 7S54; X-ray; 1.79 A; A/B=185-199.
DR PDBsum; 1IJA; -.
DR PDBsum; 1T2O; -.
DR PDBsum; 1T2P; -.
DR PDBsum; 1T2W; -.
DR PDBsum; 2KID; -.
DR PDBsum; 6R1V; -.
DR PDBsum; 7S54; -.
DR AlphaFoldDB; Q2FV99; -.
DR BMRB; Q2FV99; -.
DR SMR; Q2FV99; -.
DR STRING; 1280.SAXN108_2777; -.
DR MEROPS; C60.001; -.
DR EnsemblBacteria; ABD31836; ABD31836; SAOUHSC_02834.
DR GeneID; 3921273; -.
DR KEGG; sao:SAOUHSC_02834; -.
DR PATRIC; fig|93061.5.peg.2564; -.
DR eggNOG; COG3764; Bacteria.
DR HOGENOM; CLU_1405331_0_0_9; -.
DR OMA; MRADQKM; -.
DR Proteomes; UP000008816; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06165; Sortase_A; 1.
DR Gene3D; 2.40.260.10; -; 1.
DR InterPro; IPR005754; Sortase.
DR InterPro; IPR042007; Sortase_A.
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 3D-structure; Cell membrane; Hydrolase; Membrane; Metal-binding; Protease;
KW Reference proteome; Thiol protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..206
FT /note="Sortase A"
FT /id="PRO_0000445268"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11371637"
FT TRANSMEM 7..24
FT /note="Helical; Note=Membrane anchor"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:11371637"
FT TOPO_DOM 25..206
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:11371637"
FT REGION 49..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 120
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:11371637,
FT ECO:0000305|PubMed:11714722, ECO:0000305|PubMed:15117963,
FT ECO:0000305|PubMed:15247224, ECO:0000305|PubMed:17518446"
FT ACT_SITE 184
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000305|PubMed:11371637,
FT ECO:0000305|PubMed:11714722, ECO:0000305|PubMed:15117963,
FT ECO:0000305|PubMed:15247224, ECO:0000305|PubMed:17518446"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19592495,
FT ECO:0000305|PubMed:16269411"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19592495,
FT ECO:0000305|PubMed:16269411"
FT BINDING 112
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19592495,
FT ECO:0000305|PubMed:16269411"
FT BINDING 114
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19592495,
FT ECO:0000305|PubMed:16269411"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:19592495,
FT ECO:0000305|PubMed:16269411"
FT SITE 197
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:15117963,
FT ECO:0000305|PubMed:15247224, ECO:0000305|PubMed:17518446"
FT MUTAGEN 97
FT /note="L->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:19592495"
FT MUTAGEN 98
FT /note="N->A,Q: No change in sortase activity."
FT /evidence="ECO:0000269|PubMed:15247224"
FT MUTAGEN 104
FT /note="A->G: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:19592495"
FT MUTAGEN 108
FT /note="E->A: Retains enzymatic activity. Shows reduced
FT Ca(2+) sensitivity."
FT /evidence="ECO:0000269|PubMed:16269411"
FT MUTAGEN 118
FT /note="A->G: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:19592495"
FT MUTAGEN 120
FT /note="H->A: Almost loss or loss of activity."
FT /evidence="ECO:0000269|PubMed:11714722,
FT ECO:0000269|PubMed:17518446"
FT MUTAGEN 120
FT /note="H->Q: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:17518446"
FT MUTAGEN 132
FT /note="N->A: Does not affect dimerization of the full-
FT length protein. Disrupts dimerization; when associated with
FT A-137 and A-143."
FT /evidence="ECO:0000269|PubMed:26129884"
FT MUTAGEN 137
FT /note="K->A: Does not affect dimerization of the full-
FT length protein. Disrupts dimerization; when associated with
FT A-132 and A-143."
FT /evidence="ECO:0000269|PubMed:26129884"
FT MUTAGEN 143
FT /note="Y->A: Does not affect dimerization of the full-
FT length protein. Disrupts dimerization; when associated with
FT A-132 and A-137."
FT /evidence="ECO:0000269|PubMed:26129884"
FT MUTAGEN 170
FT /note="D->A: Retains enzymatic activity. No change in
FT dependence on Ca(2+)."
FT /evidence="ECO:0000269|PubMed:16269411"
FT MUTAGEN 171
FT /note="E->A: Retains enzymatic activity. Shows reduced
FT Ca(2+) sensitivity."
FT /evidence="ECO:0000269|PubMed:16269411"
FT MUTAGEN 180
FT /note="T->A: Decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:17518446"
FT MUTAGEN 181
FT /note="L->A: Decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:17518446"
FT MUTAGEN 182
FT /note="I->A,S: Decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:17518446"
FT MUTAGEN 183
FT /note="T->A: Strong decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:17518446"
FT MUTAGEN 184
FT /note="C->A: Abolishes sortase activity."
FT /evidence="ECO:0000269|PubMed:10535938,
FT ECO:0000269|PubMed:11714722, ECO:0000269|PubMed:17518446"
FT MUTAGEN 184
FT /note="C->H: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17518446"
FT MUTAGEN 184
FT /note="C->R: Abolishes sortase processing; when associated
FT with C-197."
FT /evidence="ECO:0000269|PubMed:15247224"
FT MUTAGEN 184
FT /note="C->S: Retains low levels of activity."
FT /evidence="ECO:0000269|PubMed:17518446"
FT MUTAGEN 185
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:17518446"
FT MUTAGEN 186
FT /note="D->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:17518446"
FT MUTAGEN 194
FT /note="W->A: Decreases the transpeptidase activity."
FT /evidence="ECO:0000269|PubMed:11714722"
FT MUTAGEN 197
FT /note="R->A,K: Strong decrease in catalytic efficiency.
FT Does not affect substrate cleavage specificity. Severe
FT decrease in sortase transpeptidase activity."
FT /evidence="ECO:0000269|PubMed:15247224,
FT ECO:0000269|PubMed:17518446"
FT MUTAGEN 197
FT /note="R->C: Abolishes sortase processing; when associated
FT with R-184."
FT /evidence="ECO:0000269|PubMed:15247224"
FT MUTAGEN 197
FT /note="R->H: Does not affect substrate cleavage
FT specificity. Severe decrease in sortase transpeptidase
FT activity."
FT /evidence="ECO:0000269|PubMed:15247224"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6R1V"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6R1V"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:6R1V"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:6R1V"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:6R1V"
FT HELIX 94..99
FT /evidence="ECO:0007829|PDB:6R1V"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:6R1V"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:6R1V"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:6R1V"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6R1V"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:6R1V"
FT STRAND 149..161
FT /evidence="ECO:0007829|PDB:6R1V"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:6R1V"
FT STRAND 174..187
FT /evidence="ECO:0007829|PDB:6R1V"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:6R1V"
FT STRAND 194..204
FT /evidence="ECO:0007829|PDB:6R1V"
SQ SEQUENCE 206 AA; 23541 MW; DC3E65C51E145C7B CRC64;
MKKWTNRLMT IAGVVLILVA AYLFAKPHID NYLHDKDKDE KIEQYDKNVK EQASKDKKQQ
AKPQIPKDKS KVAGYIEIPD ADIKEPVYPG PATPEQLNRG VSFAEENESL DDQNISIAGH
TFIDRPNYQF TNLKAAKKGS MVYFKVGNET RKYKMTSIRD VKPTDVGVLD EQKGKDKQLT
LITCDDYNEK TGVWEKRKIF VATEVK
