ID   SRTA_STRA3              Reviewed;         247 AA.
AC   Q8E5N2;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Sortase A {ECO:0000305};
DE            EC=3.4.22.- {ECO:0000305};
GN   Name=strA {ECO:0000303|PubMed:15908360};
GN   OrderedLocusNames=gbs0949 {ECO:0000312|EMBL:CAD46608.1};
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
RN   [2]
RP   FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=NEM316;
RX   PubMed=15908360; DOI=10.1128/iai.73.6.3342-3350.2005;
RA   Lalioui L., Pellegrini E., Dramsi S., Baptista M., Bourgeois N.,
RA   Doucet-Populaire F., Rusniok C., Zouine M., Glaser P., Kunst F., Poyart C.,
RA   Trieu-Cuot P.;
RT   "The SrtA sortase of Streptococcus agalactiae is required for cell wall
RT   anchoring of proteins containing the LPXTG motif, for adhesion to
RT   epithelial cells, and for colonization of the mouse intestine.";
RL   Infect. Immun. 73:3342-3350(2005).
CC   -!- FUNCTION: Transpeptidase that anchors surface proteins to the cell
CC       wall. Recognizes and modifies its substrate by proteolytic cleavage of
CC       a C-terminal sorting signal. Following cleavage, a covalent
CC       intermediate is formed via a thioester bond between the sortase and its
CC       substrate, which is then transferred and covalently attached to the
CC       cell wall. 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 (By similarity). Essential for adherence to eukaryotic cells
CC       and for binding to fibronectin and fibrinogen (PubMed:15908360).
CC       {ECO:0000250|UniProtKB:Q2FV99, ECO:0000269|PubMed:15908360}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2FV99};
CC       Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q2FV99}.
CC   -!- DISRUPTION PHENOTYPE: Mutant is unable to anchor the C5a peptidase
CC       (ScpB) and Alp2 to the cell wall. Mutant is also impaired for binding
CC       to the major extracellular matrix components fibronectin and fibrinogen
CC       and displays a significant reduction in adherence to human and murine
CC       epithelial cells. Inactivation of the gene has no effect on the
CC       virulence in a neonatal rat model but strongly impairs the capacity of
CC       the strain to colonize the intestines of gnotobiotic mice in a
CC       competition assay. {ECO:0000269|PubMed:15908360}.
CC   -!- SIMILARITY: Belongs to the bacterial sortase family. Class A subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL766848; CAD46608.1; -; Genomic_DNA.
DR   RefSeq; WP_001244677.1; NC_004368.1.
DR   AlphaFoldDB; Q8E5N2; -.
DR   SMR; Q8E5N2; -.
DR   STRING; 211110.gbs0949; -.
DR   MEROPS; C60.006; -.
DR   EnsemblBacteria; CAD46608; CAD46608; CAD46608.
DR   KEGG; san:gbs0949; -.
DR   eggNOG; COG3764; Bacteria.
DR   HOGENOM; CLU_045680_4_2_9; -.
DR   OMA; MRADQKM; -.
DR   Proteomes; UP000000823; 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   Cell membrane; Hydrolase; Membrane; Protease; Thiol protease;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..247
FT                   /note="Sortase A"
FT                   /id="PRO_0000445347"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        10..30
FT                   /note="Helical; Note=Membrane anchor"
FT                   /evidence="ECO:0000255, ECO:0000305"
FT   TOPO_DOM        31..247
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        140
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FV99"
FT   ACT_SITE        206
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FV99"
FT   SITE            214
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:Q2FV99"
SQ   SEQUENCE   247 AA;  27504 MW;  550B43FBEAFAE504 CRC64;
     MRNKKKLHGF FNFVRWLLVV LLIIVGLALV FNKPIRNAFI AHQSNHYQIS RVSKKTIEKN
     KKSKTSYDFS SVKSISTESI LSAQTKSHNL PVIGGIAIPD VEINLPIFKG LGNTELSYGA
     GTMKENQIMG GQNNYALASH HVFGLTGSSK MLFSPLEHAK KGMKVYLTDK SKVYTYTITE
     ISKVTPEHVE VIDDTPGKSQ LTLVTCTDPE ATERIIVHAE LEKTGEFSTA DESILKAFSK
     KYNQINL