SRTB_LISMO
ID SRTB_LISMO Reviewed; 246 AA.
AC Q8Y588;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Sortase B {ECO:0000303|PubMed:11929538};
DE EC=3.4.22.- {ECO:0000305|PubMed:19129190};
GN Name=srtB {ECO:0000303|PubMed:11929538}; OrderedLocusNames=lmo2181;
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 IDENTIFICATION.
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 [3]
RP FUNCTION, INDUCTION, OPERON, 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 [4]
RP INDUCTION BY IRON-DEPLETION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=15661014; DOI=10.1111/j.1365-2958.2004.04436.x;
RA Newton S.M., Klebba P.E., Raynaud C., Shao Y., Jiang X., Dubail I.,
RA Archer C., Frehel C., Charbit A.;
RT "The svpA-srtB locus of Listeria monocytogenes: fur-mediated iron
RT regulation and effect on virulence.";
RL Mol. Microbiol. 55:927-940(2005).
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 DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=16430693; DOI=10.1111/j.1365-2958.2005.05015.x;
RA Jin B., Newton S.M., Shao Y., Jiang X., Charbit A., Klebba P.E.;
RT "Iron acquisition systems for ferric hydroxamates, haemin and haemoglobin
RT in Listeria monocytogenes.";
RL Mol. Microbiol. 59:1185-1198(2006).
RN [7]
RP FUNCTION, PROBABLE CATALYTIC ACTIVITY, AND IDENTIFICATION OF SORTING
RP SIGNAL.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=19129190; DOI=10.1074/jbc.m807989200;
RA Mariscotti J.F., Garcia-del Portillo F., Pucciarelli M.G.;
RT "The Listeria monocytogenes sortase-B recognizes varied amino acids at
RT position 2 of the sorting motif.";
RL J. Biol. Chem. 284:6140-6146(2009).
RN [8]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=21545655; DOI=10.1111/j.1365-2958.2011.07667.x;
RA Xiao Q., Jiang X., Moore K.J., Shao Y., Pi H., Dubail I., Charbit A.,
RA Newton S.M., Klebba P.E.;
RT "Sortase independent and dependent systems for acquisition of haem and
RT haemoglobin in Listeria monocytogenes.";
RL Mol. Microbiol. 80:1581-1597(2011).
RN [9] {ECO:0007744|PDB:5JCV}
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 64-243.
RG Center for Structural Genomics of Infectious Diseases (CSGID);
RA Osipiuk J., Zhou M., Grimshaw S., Anderson W.F., Joachimiak A.;
RT "Sortase B from Listeria monocytogenes.";
RL Submitted (APR-2016) to the PDB data bank.
CC -!- FUNCTION: Transpeptidase that anchors surface proteins to the cell wall
CC (Probable) (PubMed:16247833, PubMed:19129190). Recognizes and modifies
CC its 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 (Probable). Catalyzes a cell
CC wall sorting reaction in which a surface protein with the consensus
CC sorting signal NP(Q/K)(T/S)(N/G/S)(D/A) is cleaved between the fourth
CC and fifth residues, and the fourth position is linked to the cell wall
CC (Probable) (PubMed:19129190). This is not the major sortase in
CC Listeria, it seems to anchor only 2 proteins, Hbp2 (SvpA) and Hbp1
CC (PubMed:15028680, PubMed:16247833). {ECO:0000269|PubMed:15028680,
CC ECO:0000269|PubMed:16247833, ECO:0000269|PubMed:19129190,
CC ECO:0000305|PubMed:15028680, ECO:0000305|PubMed:16247833}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Strongly expressed in mid-log phase, cotranscribed with
CC lmo2182 and lmo2180, the sixth gene in a possible lmo2186-lmo2180
CC operon (PubMed:15028680). Induced under iron-deficient conditions and
CC when fur (lmo1956, AC Q8Y5U9) is deleted (Probable). Induced when
CC bacteria are grown in human cell lines (Probable). Decreased hemin-
CC binding and hemin uptake by whole bacteria (PubMed:21545655).
CC {ECO:0000269|PubMed:15028680, ECO:0000269|PubMed:21545655,
CC ECO:0000305|PubMed:15661014}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in growth, no change in cell
CC wall-anchoring of InlA, no effect on bacterial growth within host cells
CC nor on virulence in a mouse infection model (PubMed:15028680). Loss of
CC cell wall-anchoring of Hbp2 (SvpA); Hbp2 is still secreted and runs
CC with an apparent lower molecular weight in gels (PubMed:15028680). A
CC double srtA-srtB deletion mutant has no cell wall-anchored proteins
CC (PubMed:15028680). No cell wall anchoring of Hbp1 or Hbp2 (SvpA)
CC (PubMed:16247833). Does not impair iron transport (PubMed:15661014,
CC PubMed:16430693). Decreased binding and uptake of hemin at low (0.5 uM
CC and 5 uM) but not high hemin concentrations (at 50 uM no effect is
CC seen) (PubMed:21545655). {ECO:0000269|PubMed:15028680,
CC ECO:0000269|PubMed:15661014, ECO:0000269|PubMed:16247833,
CC ECO:0000269|PubMed:16430693, ECO:0000269|PubMed:21545655}.
CC -!- SIMILARITY: Belongs to the bacterial sortase family. Class B subfamily.
CC {ECO:0000305}.
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DR EMBL; AL591982; CAD00259.1; -; Genomic_DNA.
DR PIR; AE1347; AE1347.
DR RefSeq; NP_465705.1; NC_003210.1.
DR RefSeq; WP_010989918.1; NZ_CP023861.1.
DR PDB; 5JCV; X-ray; 2.23 A; A=64-243.
DR PDBsum; 5JCV; -.
DR AlphaFoldDB; Q8Y588; -.
DR SMR; Q8Y588; -.
DR STRING; 169963.lmo2181; -.
DR MEROPS; C60.002; -.
DR PaxDb; Q8Y588; -.
DR EnsemblBacteria; CAD00259; CAD00259; CAD00259.
DR GeneID; 984655; -.
DR KEGG; lmo:lmo2181; -.
DR PATRIC; fig|169963.11.peg.2233; -.
DR eggNOG; COG4509; Bacteria.
DR HOGENOM; CLU_034078_3_0_9; -.
DR OMA; NENFFNA; -.
DR PhylomeDB; Q8Y588; -.
DR BioCyc; LMON169963:LMO2181-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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0071281; P:cellular response to iron ion; IEP:CollecTF.
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..246
FT /note="Sortase B"
FT /id="PRO_0000445907"
FT TRANSMEM 5..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:5JCV"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:5JCV"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5JCV"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:5JCV"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:5JCV"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:5JCV"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:5JCV"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:5JCV"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:5JCV"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:5JCV"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:5JCV"
FT STRAND 167..180
FT /evidence="ECO:0007829|PDB:5JCV"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:5JCV"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:5JCV"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5JCV"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:5JCV"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:5JCV"
SQ SEQUENCE 246 AA; 28627 MW; 9E3E72C0B486D3F2 CRC64;
MKIKSFLGKS LTLVVLGVFL FSGWKIGMEL YENKHNQTIL DDAKAVYTKD AATTNVNGEV
RDELRDLQKL NKDMVGWLTI IDTEIDYPIL QSKDNDYYLH HNYKNEKARA GSIFKDYRNT
NEFLDKNTII YGHNMKDGSM FADLRKYLDK DFLVAHPTFS YESGLTNYEV EIFAVYETTT
DFYYIETEFP ETTDFEDYLQ KVKQQSVYTS NVKVSGKDRI ITLSTCDTEK DYEKGRMVIQ
GKLVTK
