SRTA_BACAN
ID SRTA_BACAN Reviewed; 210 AA.
AC P0DPQ5;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Sortase A {ECO:0000305};
DE EC=3.4.22.- {ECO:0000305};
GN Name=srtA {ECO:0000303|PubMed:15968076, ECO:0000303|PubMed:16041044};
GN OrderedLocusNames=BAS0654 {ECO:0000312|EMBL:AAT52982.1};
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Sterne;
RX PubMed=16041044; DOI=10.1128/iai.73.8.5222-5228.2005;
RA Zink S.D., Burns D.L.;
RT "Importance of srtA and srtB for growth of Bacillus anthracis in
RT macrophages.";
RL Infect. Immun. 73:5222-5228(2005).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Sterne;
RX PubMed=15968076; DOI=10.1128/jb.187.13.4646-4655.2005;
RA Gaspar A.H., Marraffini L.A., Glass E.M., Debord K.L., Ton-That H.,
RA Schneewind O.;
RT "Bacillus anthracis sortase A (SrtA) anchors LPXTG motif-containing surface
RT proteins to the cell wall envelope.";
RL J. Bacteriol. 187:4646-4655(2005).
RN [4] {ECO:0007744|PDB:2KW8}
RP STRUCTURE BY NMR OF 57-201, AND DOMAIN.
RX PubMed=20489200; DOI=10.1074/jbc.m110.135434;
RA Weiner E.M., Robson S., Marohn M., Clubb R.T.;
RT "The sortase A enzyme that attaches proteins to the cell wall of Bacillus
RT anthracis contains an unusual active site architecture.";
RL J. Biol. Chem. 285:23433-23443(2010).
RN [5] {ECO:0007744|PDB:2RUI}
RP STRUCTURE BY NMR OF 57-201 IN COMPLEX WITH A LPXTG SORTING SIGNAL ANALOG,
RP DOMAIN, AND MUTAGENESIS OF SER-59; ILE-61 AND CYS-187.
RX PubMed=26324714; DOI=10.1074/jbc.m115.670984;
RA Chan A.H., Yi S.W., Terwilliger A.L., Maresso A.W., Jung M.E., Clubb R.T.;
RT "Structure of the Bacillus anthracis sortase A enzyme bound to its sorting
RT signal: a flexible amino-terminal appendage modulates substrate access.";
RL J. Biol. Chem. 290:25461-25474(2015).
CC -!- FUNCTION: Transpeptidase that anchors surface proteins to the cell wall
CC (PubMed:15968076). Recognizes and modifies its substrate by proteolytic
CC cleavage of 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 (PubMed:15968076). This sortase recognizes a Leu-Pro-x-Thr-
CC Gly (LPXTG) motif, which is cleaved by the sortase between the
CC threonine and glycine residues (PubMed:15968076). Important for growth
CC in macrophages. May be critical in the early stages of inhalation
CC anthrax (PubMed:16041044). {ECO:0000269|PubMed:15968076,
CC ECO:0000269|PubMed:16041044}.
CC -!- ACTIVITY REGULATION: Inhibited by thiol-reactive reagents.
CC {ECO:0000269|PubMed:15968076}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q2FV99};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q2FV99}.
CC -!- DEVELOPMENTAL STAGE: Expressed in vegetative cells.
CC {ECO:0000269|PubMed:15968076}.
CC -!- DOMAIN: Contains a unique N-terminal appendage positioned within the
CC active site and in contact with catalytically essential histidine
CC residue (PubMed:20489200). This appendage modulates substrate access to
CC the enzyme. It may increase the efficiency of protein display by
CC reducing the unproductive hydrolytic cleavage of enzyme-protein
CC covalent intermediates that form during the cell wall anchoring
CC reaction (PubMed:26324714). {ECO:0000269|PubMed:20489200,
CC ECO:0000269|PubMed:26324714}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene results in dramatic
CC attenuation of the growth of the bacteria within J774A.1 cells, a mouse
CC macrophage-like cell line (PubMed:16041044). Disruption does not affect
CC the development of acute anthrax disease in the A/J mouse model
CC (PubMed:15968076). {ECO:0000269|PubMed:15968076,
CC ECO:0000269|PubMed:16041044}.
CC -!- SIMILARITY: Belongs to the bacterial sortase family. Class A subfamily.
CC {ECO:0000305}.
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DR EMBL; AE017225; AAT52982.1; -; Genomic_DNA.
DR RefSeq; WP_001041717.1; NZ_WXXJ01000017.1.
DR RefSeq; YP_026931.1; NC_005945.1.
DR PDB; 2KW8; NMR; -; A=57-210.
DR PDB; 2RUI; NMR; -; A=57-210.
DR PDBsum; 2KW8; -.
DR PDBsum; 2RUI; -.
DR AlphaFoldDB; P0DPQ5; -.
DR SMR; P0DPQ5; -.
DR STRING; 261594.GBAA_0688; -.
DR GeneID; 45020747; -.
DR KEGG; bat:BAS0654; -.
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; Thiol protease;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..210
FT /note="Sortase A"
FT /id="PRO_0000445346"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 6..26
FT /note="Helical; Note=Membrane anchor"
FT /evidence="ECO:0000255, ECO:0000305"
FT TOPO_DOM 27..210
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT ACT_SITE 126
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q2FV99"
FT ACT_SITE 187
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q2FV99"
FT SITE 196
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q2FV99"
FT MUTAGEN 59
FT /note="S->G: Decreases sortase-mediated cell wall protein
FT anchoring."
FT /evidence="ECO:0000269|PubMed:26324714"
FT MUTAGEN 61
FT /note="I->A: Decreases sortase-mediated cell wall protein
FT anchoring."
FT /evidence="ECO:0000269|PubMed:26324714"
FT MUTAGEN 187
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:26324714"
SQ SEQUENCE 210 AA; 23151 MW; 48D40658C030137E CRC64;
MNKQRIYSIV AILLFVVGGV LIGKPFYDGY QAEKKQTENV QAVQKMDYEK HETEFVDASK
IDQPDLAEVA NASLDKKQVI GRISIPSVSL ELPVLKSSTE KNLLSGAATV KENQVMGKGN
YALAGHNMSK KGVLFSDIAS LKKGDKIYLY DNENEYEYAV TGVSEVTPDK WEVVEDHGKD
EITLITCVSV KDNSKRYVVA GDLVGTKAKK
