ID   ZMPC_STRPN              Reviewed;        1856 AA.
AC   Q97T80;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Zinc metalloprotease ZmpC;
DE            EC=3.4.24.-;
DE   AltName: Full=MMP-9 protease;
DE   Flags: Precursor;
GN   Name=zmpC; OrderedLocusNames=SP_0071;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [2]
RP   ROLE IN VIRULENCE.
RX   PubMed=12841855; DOI=10.1186/1471-2180-3-14;
RA   Chiavolini D., Memmi G., Maggi T., Iannelli F., Pozzi G., Oggioni M.R.;
RT   "The three extra-cellular zinc metalloproteinases of Streptococcus
RT   pneumoniae have a different impact on virulence in mice.";
RL   BMC Microbiol. 3:14-14(2003).
RN   [3]
RP   FUNCTION.
RX   PubMed=12864860; DOI=10.1046/j.1365-2958.2003.03596.x;
RA   Oggioni M.R., Memmi G., Maggi T., Chiavolini D., Iannelli F., Pozzi G.;
RT   "Pneumococcal zinc metalloproteinase ZmpC cleaves human matrix
RT   metalloproteinase 9 and is a virulence factor in experimental pneumonia.";
RL   Mol. Microbiol. 49:795-805(2003).
CC   -!- FUNCTION: Zinc metalloproteinase that specifically cleaves human matrix
CC       metalloproteinase 9 (MMP-9), leading to its activation. May play a role
CC       in pneumococcal virulence and pathogenicity in the lung.
CC       {ECO:0000269|PubMed:12841855, ECO:0000269|PubMed:12864860}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Secreted,
CC       cell wall {ECO:0000250}; Peptidoglycan-anchor {ECO:0000250}.
CC   -!- PTM: The Gram-positive cell-wall anchor motif LPXTG is located in the
CC       N-terminal part, in contrast to such motifs in other known
CC       streptococcal and staphylococcal proteins. The protease could be
CC       cleaved by the sortase and anchored in the membrane via the two
CC       potential N-terminal transmembrane domains, whereas the propeptide
CC       located prior to the LPXTG motif would remain attached to the cell wall
CC       peptidoglycan by an amide bond (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M26 family. {ECO:0000305}.
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DR   EMBL; AE005672; AAK74260.1; -; Genomic_DNA.
DR   PIR; C95008; C95008.
DR   RefSeq; WP_000088129.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; Q97T80; -.
DR   SMR; Q97T80; -.
DR   STRING; 170187.SP_0071; -.
DR   MEROPS; M26.003; -.
DR   PRIDE; Q97T80; -.
DR   EnsemblBacteria; AAK74260; AAK74260; SP_0071.
DR   KEGG; spn:SP_0071; -.
DR   eggNOG; COG3583; Bacteria.
DR   OMA; IKTRVYS; -.
DR   PhylomeDB; Q97T80; -.
DR   BioCyc; SPNE170187:G1FZB-75-MON; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR011098; G5_dom.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR011505; Peptidase_M26_C_dom.
DR   InterPro; IPR008006; Peptidase_M26_N_dom.
DR   InterPro; IPR005877; YSIRK_signal_dom.
DR   Pfam; PF07501; G5; 1.
DR   Pfam; PF07580; Peptidase_M26_C; 1.
DR   Pfam; PF05342; Peptidase_M26_N; 1.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   SMART; SM01208; G5; 1.
DR   TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR   PROSITE; PS51109; G5; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell wall; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Peptidoglycan-anchor; Protease; Secreted; Signal; Transmembrane;
KW   Transmembrane helix; Virulence; Zinc.
FT   SIGNAL          1..42
FT                   /evidence="ECO:0000255"
FT   PROPEP          43..95
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026845"
FT   CHAIN           96..1856
FT                   /note="Zinc metalloprotease ZmpC"
FT                   /id="PRO_0000026846"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        153..1856
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          417..496
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT   REGION          254..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           92..96
FT                   /note="LPXTG sorting signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT   COMPBIAS        254..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..332
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1503
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         1502
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1506
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         1526
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         95
FT                   /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ   SEQUENCE   1856 AA;  206737 MW;  FEB61BA533888D55 CRC64;
     MSRKSIGEKR HSFSMRKLSV GLVSVTVSSF FLMSQGIQSV SADNMESPIH YKYMTEGKLT
     DEEKSLLVEA LPQLAEESDD TYYLVYRSQQ FLPNTGFNPT VGTFLFTAGL SLLVLLVSKR
     ENGKKRLVHF LLLTSMGVQL LPASAFGLTS QILSAYNSQL SIGVGEHLPE PLKIEGYQYI
     GYIKTKKQDN TELSRTVDGK YSAQRDSQPN STKTSDVVHS ADLEWNQGQG KVSLQGEASG
     DDGLSEKSSI AADNLSSNDS FASQVEQNPD HKGESVVRPT VPEQGNPVSA TTVQSAEEEV
     LATTNDRPEY KLPLETKGTQ EPGHEGEAAV REDLPVYTKP LETKGTQGPG HEGEAAVREE
     EPAYTEPLAT KGTQEPGHEG KATVREETLE YTEPVATKGT QEPEHEGEAA VEEELPALEV
     TTRNRTEIQN IPYTTEEIQD PTLLKNRRKI ERQGQAGTRT IQYEDYIVNG NVVETKEVSR
     TEVAPVNEVV KVGTLVKVKP TVEITNLTKV ENKKSITVSY NLIDTTSAYV SAKTQVFHGD
     KLVKEVDIEN PAKEQVISGL DYYTPYTVKT HLTYNLGENN EENTETSTQD FQLEYKKIEI
     KDIDSVELYG KENDRYRRYL SLSEAPTDTA KYFVKVKSDR FKEMYLPVKS ITENTDGTYK
     VTVAVDQLVE EGTDGYKDDY TFTVAKSKAE QPGVYTSFKQ LVTAMQSNLS GVYTLASDMT
     ADEVSLGDKQ TSYLTGAFTG SLIGSDGTKS YAIYDLKKPL FDTLNGATVR DLDIKTVSAD
     SKENVAALAK AANSANINNV AVEGKISGAK SVAGLVASAT NTVIENSSFT GKLIANHQDS
     NKNDTGGIVG NITGNSSRVN KVRVDALIST NARNNNQTAG GIVGRLENGA LISNSVATGE
     IRNGQGYSRV GGIVGSTWQN GRVNNVVSNV DVGDGYVITG DQYAAADVKN ASTSVDNRKA
     DRFATKLSKD QIDAKVADYG ITVTLDDTGQ DLKRNLREVD YTRLNKAEAE RKVAYSNIEK
     LMPFYNKDLV VHYGNKVATT DKLYTTELLD VVPMKDDEVV TDINNKKNSI NKVMLHFKDN
     TVEYLDVTFK ENFINSQVIE YNVTGKEYIF TPEAFVSDYT AITNNVLSDL QNVTLNSEAT
     KKVLGAANDA ALDNLYLDRQ FEEVKANIAE HLRKVLAMDK SINTTGDGVV EYVSEKIKNN
     KEAFMLGLTY MNRWYDINYG KMNTKDLSTY KFDFNGNNET STLDTIVALG NSGLDNLRAS
     NTVGLYANKL ASVKGEDSVF DFVEAYRKLF LPNKTNNEWF KENTKAYIVE MKSDIAEVRE
     KQESPTADRK YSLGVYDRIS APSWGHKSML LPLLTLPEES VYISSNMSTL AFGSYERYRD
     SVDGVILSGD ALRTYVRNRV DIAAKRHRDH YDIWYNLLDS ASKEKLFRSV IVYDGFNVKD
     ETGRTYWARL TDKNIGSIKE FFGPVGKWYE YNSSAGAYAN GSLTHFVLDR LLDAYGTSVY
     THEMVHNSDS AIYFEGNGRR EGLGAELYAL GLLQSVDSVN SHILALNTLY KAEKDDLNRL
     HTYNPVERFD SDEALQSYMH GSYDVMYTLD AMEAKAILAQ NNDVKKKWFR KIENYYVRDT
     RHNKDTHAGN KVRPLTDEEV ANLTSLNSLI DNDIINRRSY DDSREYKRNG YYTISMFSPV
     YAALSNSKGA PGDIMFRKIA YELLAEKGYH KGFLPYVSNQ YGAEAFASGS KTFSSWHGRD
     VALVTDDLVF KKVFNGEYSS WADFKKAMFK QRIDKQDNLK PITIQYELGN PNSTKEVTIT
     TAAQMQQLIN EAAAKDITNI DRATSHTPAS WVHLLKQKIY NAYLRTTDDF RNSIYK