SRTB_STAA8
ID SRTB_STAA8 Reviewed; 244 AA.
AC Q2FZE3;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Sortase B {ECO:0000303|PubMed:11830639};
DE EC=3.4.22.71 {ECO:0000269|PubMed:24519933};
GN Name=srtB {ECO:0000303|PubMed:11830639}; OrderedLocusNames=SAOUHSC_01088;
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, CATALYTIC ACTIVITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Newman, and RN4220;
RX PubMed=11830639; DOI=10.1073/pnas.032523999;
RA Mazmanian S.K., Ton-That H., Su K., Schneewind O.;
RT "An iron-regulated sortase anchors a class of surface protein during
RT Staphylococcus aureus pathogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2293-2298(2002).
RN [3]
RP FUNCTION.
RC STRAIN=RN4220;
RX PubMed=15718231; DOI=10.1074/jbc.m500071200;
RA Marraffini L.A., Schneewind O.;
RT "Anchor structure of staphylococcal surface proteins. V. Anchor structure
RT of the sortase B substrate IsdC.";
RL J. Biol. Chem. 280:16263-16271(2005).
RN [4]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 29213 / Wichita;
RX PubMed=29690584; DOI=10.3390/molecules23040977;
RA Wang G., Wang X., Sun L., Gao Y., Niu X., Wang H.;
RT "Novel inhibitor discovery of Staphylococcus aureus sortase B and the
RT mechanism confirmation via molecular modeling.";
RL Molecules 23:0-0(2018).
RN [5] {ECO:0007744|PDB:1QWZ, ECO:0007744|PDB:1QX6, ECO:0007744|PDB:1QXA}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 31-244 IN COMPLEX WITH SUBSTRATE
RP AND INHIBITORS, ACTIVITY REGULATION, AND ACTIVE SITE.
RC STRAIN=MW2;
RX PubMed=14725770; DOI=10.1016/j.str.2003.11.021;
RA Zong Y., Mazmanian S.K., Schneewind O., Narayana S.V.;
RT "The structure of sortase B, a cysteine transpeptidase that tethers surface
RT protein to the Staphylococcus aureus cell wall.";
RL Structure 12:105-112(2004).
RN [6] {ECO:0007744|PDB:4LFD}
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 31-244 IN COMPLEX WITH SUBSTRATE
RP ANALOG, FUNCTION, ACTIVE SITE, REACTION MECHANISM, AND MUTAGENESIS OF
RP HIS-130; CYS-223; ASP-225 AND ARG-233.
RC STRAIN=USA300;
RX PubMed=24519933; DOI=10.1074/jbc.m113.509273;
RA Jacobitz A.W., Wereszczynski J., Yi S.W., Amer B.R., Huang G.L.,
RA Nguyen A.V., Sawaya M.R., Jung M.E., McCammon J.A., Clubb R.T.;
RT "Structural and computational studies of the Staphylococcus aureus sortase
RT B-substrate complex reveal a substrate-stabilized oxyanion hole.";
RL J. Biol. Chem. 289:8891-8902(2014).
CC -!- FUNCTION: Transpeptidase that anchors surface proteins to the cell wall
CC (PubMed:11830639, PubMed:15718231, PubMed:24519933) (Probable).
CC Recognizes and modifies its substrate by proteolytic cleavage of a C-
CC terminal sorting signal. Following cleavage, a covalent intermediate is
CC formed via a thioester bond between the sortase and its substrate,
CC which is then transferred and covalently attached to the cell wall
CC (Probable) (PubMed:24519933). This sortase recognizes an Asn-Pro-Gln-
CC Thr-Asn (NPQTN) motif in IsdC, which is cleaved by the sortase between
CC the threonine and aspargine residues; may only have 1 substrate in this
CC bacterium (Probable). May be dedicated to the process of iron
CC acquisition during bacterial infection (Probable).
CC {ECO:0000269|PubMed:11830639, ECO:0000269|PubMed:15718231,
CC ECO:0000269|PubMed:24519933, ECO:0000305|PubMed:11830639,
CC ECO:0000305|PubMed:15718231, ECO:0000305|PubMed:29690584}.
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 NPXTN motif is
CC cleaved between the Thr and Asn residue. The resulting threonine
CC carboxyl end of the protein is covalently attached to a pentaglycine
CC cross-bridge of peptidoglycan.; EC=3.4.22.71;
CC Evidence={ECO:0000269|PubMed:24519933, ECO:0000305|PubMed:11830639,
CC ECO:0000305|PubMed:14725770};
CC -!- ACTIVITY REGULATION: Inhibited by MTSET (2-(Trimethylammonium)-ethyl-
CC methanethiosulfonate) and E64 ([n- (l-3-trans-carboxyoxirane-2-
CC carbonyl)-l-leucyl]-amido(4-guanido)butane) (PubMed:14725770).
CC Inhibited by coptisine (PubMed:29690584). {ECO:0000269|PubMed:14725770,
CC ECO:0000269|PubMed:29690584}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Not expressed in the presence of extracellular iron,
CC repressed by fur in the presence of iron.
CC {ECO:0000305|PubMed:11830639}.
CC -!- DISRUPTION PHENOTYPE: Loss of cell wall anchoring of IsdC
CC (PubMed:11830639). No effect on establishment of mouse infections,
CC however reduced bacterial persistence after 9 days infection in mice
CC (using strain Newman, which is more pathogenic than RN4220)
CC (PubMed:11830639). {ECO:0000269|PubMed:11830639}.
CC -!- SIMILARITY: Belongs to the bacterial sortase family. Class B subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000253; ABD30203.1; -; Genomic_DNA.
DR RefSeq; WP_001242429.1; NZ_LS483365.1.
DR RefSeq; YP_499633.1; NC_007795.1.
DR PDB; 1QWZ; X-ray; 1.75 A; A=31-244.
DR PDB; 1QX6; X-ray; 2.70 A; A=31-244.
DR PDB; 1QXA; X-ray; 2.50 A; A=31-244.
DR PDB; 4LFD; X-ray; 2.49 A; A/B/C/D=31-244.
DR PDBsum; 1QWZ; -.
DR PDBsum; 1QX6; -.
DR PDBsum; 1QXA; -.
DR PDBsum; 4LFD; -.
DR AlphaFoldDB; Q2FZE3; -.
DR SMR; Q2FZE3; -.
DR STRING; 1280.SAXN108_1130; -.
DR ChEMBL; CHEMBL3329; -.
DR MEROPS; C60.002; -.
DR EnsemblBacteria; ABD30203; ABD30203; SAOUHSC_01088.
DR GeneID; 3919249; -.
DR KEGG; sao:SAOUHSC_01088; -.
DR PATRIC; fig|93061.5.peg.997; -.
DR eggNOG; COG4509; Bacteria.
DR HOGENOM; CLU_034078_3_0_9; -.
DR OMA; NENFFNA; -.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd05826; Sortase_B; 1.
DR Gene3D; 2.40.260.10; -; 1.
DR InterPro; IPR005754; Sortase.
DR InterPro; IPR023365; Sortase_dom-sf.
DR InterPro; IPR009835; SrtB.
DR InterPro; IPR015986; SrtB_Firmicute.
DR Pfam; PF04203; Sortase; 1.
DR PIRSF; PIRSF030150; UCP030150; 1.
DR SUPFAM; SSF63817; SSF63817; 1.
DR TIGRFAMs; TIGR03064; sortase_srtB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..244
FT /note="Sortase B"
FT /id="PRO_0000445584"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..24
FT /note="Helical; Note=Membrane anchor"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..244
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT ACT_SITE 223
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000305|PubMed:14725770"
FT SITE 233
FT /note="Transition state stablizer"
FT /evidence="ECO:0000305|PubMed:14725770,
FT ECO:0000305|PubMed:24519933"
FT MUTAGEN 130
FT /note="H->A: Loss of transpeptidation activity."
FT /evidence="ECO:0000269|PubMed:24519933"
FT MUTAGEN 223
FT /note="C->A: Loss of transpeptidation activity."
FT /evidence="ECO:0000269|PubMed:24519933"
FT MUTAGEN 225
FT /note="D->A: Non-specific protease activity."
FT /evidence="ECO:0000269|PubMed:24519933"
FT MUTAGEN 233
FT /note="R->A: Loss of transpeptidation activity."
FT /evidence="ECO:0000269|PubMed:24519933"
FT HELIX 31..52
FT /evidence="ECO:0007829|PDB:1QWZ"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:1QXA"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:1QWZ"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:1QWZ"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:1QWZ"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1QWZ"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1QWZ"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1QWZ"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1QWZ"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:1QWZ"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1QWZ"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:1QWZ"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:1QWZ"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1QWZ"
FT STRAND 163..178
FT /evidence="ECO:0007829|PDB:1QWZ"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1QXA"
FT HELIX 189..202
FT /evidence="ECO:0007829|PDB:1QWZ"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1QX6"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1QWZ"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1QXA"
FT STRAND 232..244
FT /evidence="ECO:0007829|PDB:1QWZ"
SQ SEQUENCE 244 AA; 29163 MW; 1442B260651CD877 CRC64;
MRMKRFLTIV QILLVVIIII FGYKIVQTYI EDKQERANYE KLQQKFQMLM SKHQEHVRPQ
FESLEKINKD IVGWIKLSGT SLNYPVLQGK TNHDYLNLDF EREHRRKGSI FMDFRNELKN
LNHNTILYGH HVGDNTMFDV LEDYLKQSFY EKHKIIEFDN KYGKYQLQVF SAYKTTTKDN
YIRTDFENDQ DYQQFLDETK RKSVINSDVN VTVKDRIMTL STCEDAYSET TKRIVVVAKI
IKVS
