ID   IGMDE_STRSE             Reviewed;        1141 AA.
AC   C5W022;
DT   19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=IgM protease;
DE            EC=3.4.22.-;
DE   AltName: Full=Immunoglobulin M-degrading enzyme of S.suis;
DE            Short=IdeSsuis;
DE   Flags: Precursor;
GN   Name=ide; OrderedLocusNames=SSU0496;
OS   Streptococcus suis (strain P1/7).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218494;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1/7;
RX   PubMed=19603075; DOI=10.1371/journal.pone.0006072;
RA   Holden M.T.G., Hauser H., Sanders M., Ngo T.H., Cherevach I., Cronin A.,
RA   Goodhead I., Mungall K., Quail M.A., Price C., Rabbinowitsch E., Sharp S.,
RA   Croucher N.J., Chieu T.B., Mai N.T.H., Diep T.S., Chinh N.T., Kehoe M.,
RA   Leigh J.A., Ward P.N., Dowson C.G., Whatmore A.M., Chanter N., Iversen P.,
RA   Gottschalk M., Slater J.D., Smith H.E., Spratt B.G., Xu J., Ye C.,
RA   Bentley S., Barrell B.G., Schultsz C., Maskell D.J., Parkhill J.;
RT   "Rapid evolution of virulence and drug resistance in the emerging zoonotic
RT   pathogen Streptococcus suis.";
RL   PLoS ONE 4:E6072-E6072(2009).
RN   [2]
RP   FUNCTION AS IGM PROTEASE, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP   SUBCELLULAR LOCATION, DOMAIN, AND DISRUPTION PHENOTYPE.
RC   STRAIN=10 / Serotype 2;
RX   PubMed=23243300; DOI=10.1128/jb.01875-12;
RA   Seele J., Singpiel A., Spoerry C., von Pawel-Rammingen U.,
RA   Valentin-Weigand P., Baums C.G.;
RT   "Identification of a novel host-specific IgM protease in Streptococcus
RT   suis.";
RL   J. Bacteriol. 195:930-940(2013).
CC   -!- FUNCTION: Catalyzes the specific cleavage of porcine IgM bound to the
CC       bacterial surface. Can degrade only IgM but neither IgG nor IgA, and is
CC       host specific, as it exclusively cleaves porcine IgM but not IgM from
CC       six other species, including human, mouse and a closely related member
CC       of the Suidae family. Promotes survival in porcine blood. Is thus
CC       involved in a so-far-unknown mechanism of host-pathogen interaction at
CC       an early stage of the host immune response.
CC       {ECO:0000269|PubMed:23243300}.
CC   -!- ACTIVITY REGULATION: IgM cleavage is inhibited by iodoacetamide but not
CC       by AEBSF, bestatin, E-64, Z-LVG-CHN(2), or EDTA.
CC       {ECO:0000269|PubMed:23243300}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23243300};
CC       Single-pass membrane protein {ECO:0000269|PubMed:23243300}. Secreted
CC       {ECO:0000269|PubMed:23243300}. Note=Is released into the extracellular
CC       space and remains at least transiently attached to the bacterial
CC       surface, likely via its C-terminal transmembrane domain.
CC   -!- DOMAIN: Domain encompassing residues 35-432 are sufficient for IgM
CC       cleavage. {ECO:0000269|PubMed:23243300}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose IgM-cleaving
CC       activity and show an increase of surface-bound IgM antigen. They are
CC       also significantly attenuated in survival in blood of a piglet
CC       vaccinated once with a bacterin, in comparison to the wild-type.
CC       {ECO:0000269|PubMed:23243300}.
CC   -!- SIMILARITY: Belongs to the peptidase C66 family. {ECO:0000305}.
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DR   EMBL; AM946016; CAR45112.1; -; Genomic_DNA.
DR   RefSeq; WP_011922092.1; NC_012925.1.
DR   AlphaFoldDB; C5W022; -.
DR   SMR; C5W022; -.
DR   MEROPS; C66.003; -.
DR   KEGG; ssi:SSU0496; -.
DR   HOGENOM; CLU_294903_0_0_9; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   InterPro; IPR015117; IdeS.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR005877; YSIRK_signal_dom.
DR   Pfam; PF09028; Mac-1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   TIGRFAMs; TIGR01168; YSIRK_signal; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Hydrolase; Membrane; Protease; Secreted; Signal;
KW   Thiol protease; Transmembrane; Transmembrane helix; Virulence.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..1141
FT                   /note="IgM protease"
FT                   /id="PRO_5000480020"
FT   TRANSMEM        1119..1136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          518..544
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..805
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..749
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..805
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        195
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1141 AA;  123714 MW;  FD6730AE8E72DBBA CRC64;
     MNIQERFSLR KSAVGLVSVS LLCAIYTSTV AADTVVTGVN EIIEESQVKD EVSIESEKNE
     SLDGSNIEIV EEIADNIPSP VIAEGEVAVE MKVDRGTENV VSRNDTEVTT SEQNQIEVTE
     TKEILNQTSY QTESGEQRQI IWAHGITPPA MEQSGGFVKE KYGDYLNYTA PFEAGKGYYD
     TNKSLNASFI DLNLCFAAVS SNMVHWWLEQ NSSYVERYLK EKKGTVNVEE NYAITDLRRY
     INSFQNQQNS RVFDMFKTYY GYRTNGFVSD ALVDLFINGY KPKAQGGVNL EDSQLVPDSR
     GGFFYDVFKE KKLTNRIFSG SYERFGEDVR TVLESKGLLG LTYRTLGYAT HIVTVWGAEY
     DNQGKIKAVY ITDSDDQQEQ IGLKRMGITR DASGNPRLNN HMKNNSAGAL LDYVHTIRLG
     QDLWEEYFNP LAKAKETASQ TLADTKKALD LSIQGQSELP ESMRLIYLEK LNNLYNQGIL
     SIQKAESSEM LSGALENGLN SLKSLDFPIS EVGNALAPDL PVGDRSTVSD VDSLSSQETS
     STNLEADTEN AGIIADGTNQ LHFPVEAQTT SSVEAEGDNV FEQEADTLPI IIENKDEFGS
     ELSRNMQTSE TDSLVVAVEE DVKNDEVAQV EELLESEKVE NQSSELLSDT LIVESANDKE
     EDRVEAVVSE QPDSIPHQNV EISLVEPTNV ETETVVTPIN DAATPHGSPT YIDNSVTESV
     ATPLEKDSIQ AGETEIAEPT SSESTNVETE TVVTPVNDVA TPHGSPTYID NSVTESVATP
     LEKDSIQAGE TEIAEPTSSE STNVETETVV TPVNDVATPH GSPTYIDNSV TESVATPLEK
     DSIQAGETEI AEPTSSESTS VEAELVDNSE IHAATSSVTP CGSSAYADGS TTESVATPLE
     KDSIQTGNTE IAEPTSSKST NVEAASVDNS EIHADASLTA VSSVNLDNPV IEPVAISLIG
     SKRDTNAEVE VSSLSKREVR KTNTDGLISV QSKVIKKELL ESSLAEAGSP LLEATIAQSS
     NSNSTEIGMS YQNTVLLESN NTERQVSKAE IVMEHKETEL VETVSSASEP VVLVENISQT
     SNNTIESGKN MGVQSQAGAK QILGVEQSSK VSTPTSRQIM GVGLLTLVLG SALGLLKKRR
     K