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Zinc metalloprotease ZmpB (EC 3.4.24.-)

 ZMPB_STRPN              Reviewed;        1906 AA.
Q9L7Q2; Q7D4C2;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-FEB-2005, sequence version 2.
05-JUL-2017, entry version 96.
RecName: Full=Zinc metalloprotease ZmpB;
EC=3.4.24.-;
Flags: Precursor;
Name=zmpB; OrderedLocusNames=SP_0664;
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=170187;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CELL SURFACE LOCALIZATION.
STRAIN=Serotype 4;
PubMed=10792723; DOI=10.1046/j.1365-2958.2000.01854.x;
Novak R., Charpentier E., Braun J.S., Park E., Murti S., Tuomanen E.,
Masure R.;
"Extracellular targeting of choline-binding proteins in Streptococcus
pneumoniae by a zinc metalloprotease.";
Mol. Microbiol. 36:366-376(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-334 / TIGR4;
PubMed=11463916; DOI=10.1126/science.1061217;
Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T.,
Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C.,
Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.;
"Complete genome sequence of a virulent isolate of Streptococcus
pneumoniae.";
Science 293:498-506(2001).
[3]
DISCUSSION OF FUNCTION.
PubMed=11260480; DOI=10.1046/j.1365-2958.2001.02359.x;
Berge M., Garcia P., Iannelli F., Prere M.F., Granadel C., Polissi A.,
Claverys J.-P.;
"The puzzle of zmpB and extensive chain formation, autolysis defect
and non-translocation of choline-binding proteins in Streptococcus
pneumoniae.";
Mol. Microbiol. 39:1651-1660(2001).
[4]
ROLE IN VIRULENCE.
STRAIN=ATCC BAA-334 / TIGR4;
PubMed=12841855; DOI=10.1186/1471-2180-3-14;
Chiavolini D., Memmi G., Maggi T., Iannelli F., Pozzi G.,
Oggioni M.R.;
"The three extra-cellular zinc metalloproteinases of Streptococcus
pneumoniae have a different impact on virulence in mice.";
BMC Microbiol. 3:14-14(2003).
[5]
ROLE IN INFLAMMATION.
STRAIN=Serotype 2;
PubMed=12933834; DOI=10.1128/IAI.71.9.4925-4935.2003;
Blue C.E., Paterson G.K., Kerr A.R., Berge M., Claverys J.-P.,
Mitchell T.J.;
"ZmpB, a novel virulence factor of Streptococcus pneumoniae that
induces tumor necrosis factor alpha production in the respiratory
tract.";
Infect. Immun. 71:4925-4935(2003).
-!- FUNCTION: Is a virulence factor capable of inducing inflammation
in the lower respiratory tract, by increasing tumor necrosis
factor alpha (TNF-alpha) concentration in the lungs. Also appears
to have other functions important in virulence in models of
pneumonia and septicemia. {ECO:0000269|PubMed:12841855,
ECO:0000269|PubMed:12933834}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane; Multi-pass
membrane protein. Secreted, cell wall; Peptidoglycan-anchor.
-!- PTM: The Gram-positive cell-wall anchor motif LPXTG is located in
the N-terminal part, in contrast to such motifs in other known
streptococcal and staphylococcal proteins. The protease could be
cleaved by the sortase and anchored in the membrane via the two
potential N-terminal transmembrane domains, whereas the propeptide
located prior to the LPXTG motif would remain attached to the cell
wall peptidoglycan by an amide bond.
-!- SIMILARITY: Belongs to the peptidase M26 family. {ECO:0000305}.
-!- CAUTION: Was originally (PubMed:10792723) thought to control
translocation of choline-binding proteins to the cell surface but
PubMed:11260480 failed to confirm this observation. The
conflicting observations could be explained by the fact that the
mutant strain used in PubMed:10792723 lacked capsule.
{ECO:0000305|PubMed:10792723}.
-!- SEQUENCE CAUTION:
Sequence=AAF31454.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAK74809.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF221126; AAF31454.1; ALT_INIT; Genomic_DNA.
EMBL; AE005672; AAK74809.1; ALT_INIT; Genomic_DNA.
PIR; H95076; H95076.
RefSeq; WP_000472995.1; NZ_AKVY01000001.1.
ProteinModelPortal; Q9L7Q2; -.
MEROPS; M26.002; -.
EnsemblBacteria; AAK74809; AAK74809; SP_0664.
KEGG; spn:SP_0664; -.
eggNOG; ENOG4105EEN; Bacteria.
eggNOG; ENOG410XR1H; LUCA.
HOGENOM; HOG000244602; -.
KO; K08643; -.
OMA; TQESGHE; -.
Proteomes; UP000000585; Chromosome.
GO; GO:0009986; C:cell surface; IDA:CACAO.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
InterPro; IPR019948; Gram-positive_anchor.
InterPro; IPR011505; Peptidase_M26_C_dom.
InterPro; IPR008006; Peptidase_M26_N_dom.
Pfam; PF00746; Gram_pos_anchor; 1.
Pfam; PF07580; Peptidase_M26_C; 1.
Pfam; PF05342; Peptidase_M26_N; 1.
3: Inferred from homology;
Cell wall; Complete proteome; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Peptidoglycan-anchor; Protease; Repeat; Secreted;
Signal; Transmembrane; Transmembrane helix; Virulence; Zinc.
SIGNAL 1 33 {ECO:0000255}.
PROPEP 34 76 {ECO:0000255}.
/FTId=PRO_0000026841.
CHAIN 77 1906 Zinc metalloprotease ZmpB.
/FTId=PRO_0000026842.
TRANSMEM 77 98 Helical. {ECO:0000255}.
TRANSMEM 105 127 Helical. {ECO:0000255}.
TOPO_DOM 128 1906 Extracellular. {ECO:0000255}.
REPEAT 277 291 1-1.
REPEAT 293 315 2-1.
REPEAT 361 375 1-2.
REPEAT 380 402 2-2.
REGION 277 375 2 X 15 AA repeats of K-V-E-Q-A-G-E-P-V-A-
P-R-E-D-E.
REGION 293 375 2 X 23 AA approximate repeats.
MOTIF 73 77 LPXTG sorting signal. {ECO:0000255}.
COMPBIAS 164 404 Glu-rich.
ACT_SITE 1563 1563 {ECO:0000250}.
METAL 1562 1562 Zinc. {ECO:0000250}.
METAL 1566 1566 Zinc. {ECO:0000250}.
METAL 1586 1586 Zinc. {ECO:0000250}.
MOD_RES 76 76 Pentaglycyl murein peptidoglycan amidated
threonine. {ECO:0000255}.
SEQUENCE 1906 AA; 213535 MW; 2A03CB9311E06928 CRC64;
MFKKDRFSIR KIKGVVGSVF LGSLLMAPSV VDAATYHYVN KEIISQEAKD LIQTGKPDRN
EVVYGLVYQK DQLPQTGTEA SVLTAFGLLT VGSLLLIYKR KKIASVFLVG AMGLVVLPSA
GAVDPVATLA LASREGVVEM EGYRYVGYLS GDILKTLGLD TVLEETSAKP GEVTVVEVET
PQSITNQEQA RTENQVVETE EAPKEEAPKT EESPKEEPKS EVKPTDDTLP KVEEGKEDSA
EPAPVEEVGG EVESKPEEKV AVKPESQPSD KPAEESKVEQ AGEPVAPRED EKAPVEPEKQ
PEAPEEEKAV EETPKQEEST PDTKAEETVE PKEETVNQSI EQPKVETPAV EKQTEPTEEP
KVEQAGEPVA PREDEQAPTA PVEPEKQPEV PEEEKAVEET PKPEDKIKGI GTKEPVDKSE
LNNQIDKASS VSPTDYSTAS YNALGPVLET AKGVYASEPV KQPEVNSETN KLKTAIDALN
VDKTELNNTI ADAKTKVKEH YSDRSWQNLQ TEVTKAEKVA ANTDAKQSEV NEAVEKLTAT
IEKLVELSEK PILTLTSTDK KILEREAVAK YTLENQNKTK IKSITAELKK GEEVINTVVL
TDDKVTTETI SAAFKNLEYY KEYTLSTTMI YDRGNGEETE TLENQNIQLD LKKVELKNIK
RTDLIKYENG KETNESLITT IPDDKSNYYL KITSNNQKTT LLAVKNIEET TVNGTPVYKV
TAIADNLVSR TADNKFEEEY VHYIEKPKVH EDNVYYNFKE LVEAIQNDPS KEYRLGQSMS
ARNVVPNGKS YITKEFTGKL LSSEGKQFAI TELEHPLFNV ITNATINNVN FENVEIERSG
QDNIASLANT MKGSSVITNV KITGTLSGRN NVAGFVNNMN DGTRIENVAF FGKLHSTSGN
GSHTGGIAGT NYRGIVRKAY VDATITGNKT RASLLVPKVD YGLTLDHLIG TKALLTESVV
KGKIDVSNPV EVGAIASKTW PVGTVSNSVS YAKIIRGEEL FGSNDVDDSD YASAHIKDLY
AVEGYSSGNR SFRKSKTFTK LTKEQADAKV TTFNITADKL ESDLSPLAKL NEEKAYSSIQ
DYNAEYNQAY KNLEKLIPFY NKDYIVYQGN KLNKEHHLNT KEVLSVTAMN NNEFITNLDE
ANKIIVHYAD GTKDYFNLSS SSEGLSNVKE YTITDLGIKY TPNIVQKDNT TLVNDIKSIL
ESVELQSQTM YQHLNRLGDY RVNAIKDLYL EESFTDVKEN LTNLITKLVQ NEEHQLNDSP
AARQMIRDKV EKNKAALLLG LTYLNRYYGV KFGDVNIKEL MLFKPDFYGE KVSVLDRLIE
IGSKENNIKG SRTFDAFGQV LAKYTKSGNL DAFLNYNRQL FTNIDNMNDW FIDATEDHVY
IAERASEVEE IKNSKHRAFD NLKRSHLRNT ILPLLNIDKA HLYLISNYNA IAFGSAERLG
KKSLEDIKDI VNKAADGYRN YYDFWYRLAS DNVKQRLLRD AVIPIWEGYN APGGWVEKYG
RYNTDKVYTP LREFFGPMDK YYNYNGTGAY AAIYPNSDDI RTDVKYVHLE MVGEYGISVY
THETTHVNDR AIYLGGFGHR EGTDAEAYAQ GMLQTPVTGS GFDEFGSLGI NMVFKRKNDG
NQWYITDPKT LKTREDINRY MKGYNDTLTL LDEIEAESVI SQQNKDLNSA WFKKIDREYR
DNNKLNQWDK IRNLSQEEKN ELNIQSVNDL VDQQLMTNRN PGNGIYKPEA ISYNDQSPYV
GVRMMTGIYG GNTSKGAPGA VSFKHNAFRL WGYYGYENGF LGYASNKYKQ QSKTDGESVL
SDEYIIKKIS NNTFNTIEEF KKAYFKEVKD KATKGLTTFE VNGSSVSSYD DLLTLFKEAV
KKDAETLKQE ANGNKTVSMN NTVKLKEAVY KKLLQQTNSF KTSIFK


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