SRTA_LISMO
ID SRTA_LISMO Reviewed; 222 AA.
AC Q8Y8H5;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Sortase A {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
GN Name=srtA {ECO:0000303|PubMed:11854224, ECO:0000303|PubMed:11929538};
GN OrderedLocusNames=lmo0929 {ECO:0000312|EMBL:CAC99007.1};
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11854224; DOI=10.1128/iai.70.3.1382-1390.2002;
RA Garandeau C., Reglier-Poupet H., Dubail I., Beretti J.L., Berche P.,
RA Charbit A.;
RT "The sortase SrtA of Listeria monocytogenes is involved in processing of
RT internalin and in virulence.";
RL Infect. Immun. 70:1382-1390(2002).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11929538; DOI=10.1046/j.1365-2958.2002.02798.x;
RA Bierne H., Mazmanian S.K., Trost M., Pucciarelli M.G., Liu G., Dehoux P.,
RA Jansch L., Garcia-del Portillo F., Schneewind O., Cossart P.;
RT "Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring
RT of surface proteins and affects virulence.";
RL Mol. Microbiol. 43:869-881(2002).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=15028680; DOI=10.1128/jb.186.7.1972-1982.2004;
RA Bierne H., Garandeau C., Pucciarelli M.G., Sabet C., Newton S.,
RA Garcia-del Portillo F., Cossart P., Charbit A.;
RT "Sortase B, a new class of sortase in Listeria monocytogenes.";
RL J. Bacteriol. 186:1972-1982(2004).
RN [5]
RP FUNCTION, SUBSTRATE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=16247833; DOI=10.1002/pmic.200402075;
RA Pucciarelli M.G., Calvo E., Sabet C., Bierne H., Cossart P.,
RA Garcia-del Portillo F.;
RT "Identification of substrates of the Listeria monocytogenes sortases A and
RT B by a non-gel proteomic analysis.";
RL Proteomics 5:4808-4817(2005).
RN [6]
RP FUNCTION, SUBSTRATES, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=22837151; DOI=10.2436/20.1501.01.157;
RA Mariscotti J.F., Quereda J.J., Pucciarelli M.G.;
RT "Contribution of sortase A to the regulation of Listeria monocytogenes
RT LPXTG surface proteins.";
RL Int. Microbiol. 15:43-51(2012).
RN [7]
RP 3D-STRUCTURE MODELING.
RX PubMed=21374720; DOI=10.1002/prot.22983;
RA Tian B., Eriksson L.A.;
RT "Structural changes of Listeria monocytogenes sortase A: a key to
RT understanding the catalytic mechanism.";
RL Proteins 79:1564-1572(2011).
RN [8] {ECO:0007744|PDB:5HU4}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 78-222, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF HIS-127; CYS-188 AND ARG-197.
RC STRAIN=BUG1600;
RX PubMed=26826492; DOI=10.1016/j.bcp.2016.01.018;
RA Li H., Chen Y., Zhang B., Niu X., Song M., Luo Z., Lu G., Liu B., Zhao X.,
RA Wang J., Deng X.;
RT "Inhibition of sortase A by chalcone prevents Listeria monocytogenes
RT infection.";
RL Biochem. Pharmacol. 106:19-29(2016).
CC -!- FUNCTION: Transpeptidase that anchors surface proteins to the cell wall
CC (PubMed:11854224, PubMed:11929538, PubMed:16247833, PubMed:22837151).
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). This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif,
CC which is cleaved by the sortase between the threonine and glycine
CC residues (PubMed:11929538). Involved in pathogenesis (PubMed:11854224,
CC PubMed:11929538, PubMed:15028680). May regulate the rate of synthesis
CC and/or the stability of a subset of LPXTG proteins (PubMed:22837151).
CC Not involved in cell wall-anchoring of Hbp2 (SvpA) or Hbp1
CC (PubMed:15028680, PubMed:16247833). {ECO:0000269|PubMed:11854224,
CC ECO:0000269|PubMed:11929538, ECO:0000269|PubMed:15028680,
CC ECO:0000269|PubMed:16247833, ECO:0000269|PubMed:22837151,
CC ECO:0000305|PubMed:11929538}.
CC -!- ACTIVITY REGULATION: Activity is enhanced by Zn(2+) and strongly
CC enhanced by Ca(2+). Inhibited by chalcone, a precursor of several
CC flavonoids, which blocks the SrtA active site.
CC {ECO:0000269|PubMed:26826492}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11929538};
CC Single-pass type II membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Seems to contribute mostly when the bacteria reach
CC stationary phase. {ECO:0000269|PubMed:22837151}.
CC -!- DISRUPTION PHENOTYPE: Mutant is defective in processing and surface
CC anchoring of internalins and several other LPXTG-containing proteins
CC (PubMed:11854224, PubMed:11929538, PubMed:22837151, PubMed:16247833).
CC Mutant is significantly less invasive in vitro and is attenuated in
CC virulence in a mouse model of infection (PubMed:11854224,
CC PubMed:11929538). Deletion of the gene does not affect expression of
CC the genes encoding LPXTG surface proteins (PubMed:22837151). A double
CC srtA-srtB deletion mutant has no cell wall-anchored proteins, and is as
CC impaired in virulence as a single srtA mutant (PubMed:15028680).
CC {ECO:0000269|PubMed:11854224, ECO:0000269|PubMed:11929538,
CC ECO:0000269|PubMed:15028680, ECO:0000269|PubMed:16247833,
CC ECO:0000269|PubMed:22837151}.
CC -!- SIMILARITY: Belongs to the bacterial sortase family. Class A subfamily.
CC {ECO:0000305}.
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DR EMBL; AL591977; CAC99007.1; -; Genomic_DNA.
DR PIR; AI1190; AI1190.
DR RefSeq; NP_464454.1; NC_003210.1.
DR RefSeq; WP_003722751.1; NZ_CP023861.1.
DR PDB; 5HU4; X-ray; 2.30 A; A=78-222.
DR PDBsum; 5HU4; -.
DR AlphaFoldDB; Q8Y8H5; -.
DR SMR; Q8Y8H5; -.
DR STRING; 169963.lmo0929; -.
DR MEROPS; C60.006; -.
DR PaxDb; Q8Y8H5; -.
DR EnsemblBacteria; CAC99007; CAC99007; CAC99007.
DR GeneID; 986837; -.
DR KEGG; lmo:lmo0929; -.
DR PATRIC; fig|169963.11.peg.955; -.
DR eggNOG; COG3764; Bacteria.
DR HOGENOM; CLU_045680_4_1_9; -.
DR OMA; MRADQKM; -.
DR PhylomeDB; Q8Y8H5; -.
DR BioCyc; LMON169963:LMO0929-MON; -.
DR Proteomes; UP000000817; 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; 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; Protease;
KW Reference proteome; Thiol protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..222
FT /note="Sortase A"
FT /id="PRO_0000445267"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..28
FT /note="Helical; Note=Membrane anchor"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:11929538"
FT TOPO_DOM 29..222
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT ACT_SITE 127
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q2FV99"
FT ACT_SITE 188
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q2FV99"
FT SITE 197
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q2FV99"
FT MUTAGEN 127
FT /note="H->A: Lack of transpeptidase activity."
FT /evidence="ECO:0000269|PubMed:26826492"
FT MUTAGEN 188
FT /note="C->A: Lack of transpeptidase activity. Does not bind
FT chalcone."
FT /evidence="ECO:0000269|PubMed:26826492"
FT MUTAGEN 197
FT /note="R->A: Strong decrease in transpeptidase activity.
FT Does not bind chalcone."
FT /evidence="ECO:0000269|PubMed:26826492"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:5HU4"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:5HU4"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:5HU4"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:5HU4"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:5HU4"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:5HU4"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:5HU4"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:5HU4"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:5HU4"
FT STRAND 153..168
FT /evidence="ECO:0007829|PDB:5HU4"
FT HELIX 172..175
FT /evidence="ECO:0007829|PDB:5HU4"
FT STRAND 182..193
FT /evidence="ECO:0007829|PDB:5HU4"
FT STRAND 195..209
FT /evidence="ECO:0007829|PDB:5HU4"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:5HU4"
SQ SEQUENCE 222 AA; 24712 MW; C3BC4BD8B8A4339B CRC64;
MLKKTIAIII LIIGLLLIFS PFIKNGIVKY MSGHETIEQY KASDIKKNNE KDATFDFESV
QLPSMTSVIK GAANYDKDAV VGSIAVPSVD VNLLVFKGTN TANLLAGATT MRSDQVMGKG
NYPLAGHHMR DESMLFGPIM KVKKGDKIYL TDLENLYEYT VTETKTIDET EVSVIDNTKD
ARITLITCDK PTETTKRFVA VGELEKTEKL TKELENKYFP SK
