ID ZMPB_STRPN Reviewed; 1906 AA.
AC Q9L7Q2; Q7D4C2;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=Zinc metalloprotease ZmpB;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=zmpB; OrderedLocusNames=SP_0664;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CELL SURFACE LOCALIZATION.
RC STRAIN=Serotype 4;
RX PubMed=10792723; DOI=10.1046/j.1365-2958.2000.01854.x;
RA Novak R., Charpentier E., Braun J.S., Park E., Murti S., Tuomanen E.,
RA Masure R.;
RT "Extracellular targeting of choline-binding proteins in Streptococcus
RT pneumoniae by a zinc metalloprotease.";
RL Mol. Microbiol. 36:366-376(2000).
RN [2]
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 [3]
RP DISCUSSION OF FUNCTION.
RX PubMed=11260480; DOI=10.1046/j.1365-2958.2001.02359.x;
RA Berge M., Garcia P., Iannelli F., Prere M.F., Granadel C., Polissi A.,
RA Claverys J.-P.;
RT "The puzzle of zmpB and extensive chain formation, autolysis defect and
RT non-translocation of choline-binding proteins in Streptococcus
RT pneumoniae.";
RL Mol. Microbiol. 39:1651-1660(2001).
RN [4]
RP ROLE IN VIRULENCE.
RC STRAIN=ATCC BAA-334 / TIGR4;
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 [5]
RP ROLE IN INFLAMMATION.
RC STRAIN=Serotype 2;
RX PubMed=12933834; DOI=10.1128/iai.71.9.4925-4935.2003;
RA Blue C.E., Paterson G.K., Kerr A.R., Berge M., Claverys J.-P.,
RA Mitchell T.J.;
RT "ZmpB, a novel virulence factor of Streptococcus pneumoniae that induces
RT tumor necrosis factor alpha production in the respiratory tract.";
RL Infect. Immun. 71:4925-4935(2003).
CC -!- FUNCTION: Is a virulence factor capable of inducing inflammation in the
CC lower respiratory tract, by increasing tumor necrosis factor alpha
CC (TNF-alpha) concentration in the lungs. Also appears to have other
CC functions important in virulence in models of pneumonia and septicemia.
CC {ECO:0000269|PubMed:12841855, ECO:0000269|PubMed:12933834}.
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. Membrane; Multi-pass
CC membrane protein. Secreted, cell wall; Peptidoglycan-anchor.
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.
CC -!- SIMILARITY: Belongs to the peptidase M26 family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:10792723) thought to control
CC translocation of choline-binding proteins to the cell surface but
CC PubMed:11260480 failed to confirm this observation. The conflicting
CC observations could be explained by the fact that the mutant strain used
CC in PubMed:10792723 lacked capsule. {ECO:0000305|PubMed:10792723}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF31454.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK74809.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF221126; AAF31454.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE005672; AAK74809.1; ALT_INIT; Genomic_DNA.
DR PIR; H95076; H95076.
DR RefSeq; WP_000472995.1; NZ_CP089948.1.
DR AlphaFoldDB; Q9L7Q2; -.
DR SMR; Q9L7Q2; -.
DR MEROPS; M26.002; -.
DR PaxDb; 170187-SP_0664; -.
DR EnsemblBacteria; AAK74809; AAK74809; SP_0664.
DR KEGG; spn:SP_0664; -.
DR eggNOG; COG3064; Bacteria.
DR PhylomeDB; Q9L7Q2; -.
DR BioCyc; SPNE170187:G1FZB-687-MONOMER; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0009986; C:cell surface; IDA:CACAO.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 1.20.1270.90; AF1782-like; 2.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR011505; Peptidase_M26_C_dom.
DR InterPro; IPR008006; Peptidase_M26_N_dom.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR48193:SF2; ZINC METALLOPROTEASE ZMPB; 1.
DR PANTHER; PTHR48193; ZINC METALLOPROTEASE ZMPB-RELATED; 1.
DR Pfam; PF07554; FIVAR; 2.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF07580; Peptidase_M26_C; 1.
DR Pfam; PF05342; Peptidase_M26_N; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Peptidoglycan-anchor; Protease; Reference proteome; Repeat; Secreted;
KW Signal; Transmembrane; Transmembrane helix; Virulence; Zinc.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..76
FT /evidence="ECO:0000255"
FT /id="PRO_0000026841"
FT CHAIN 77..1906
FT /note="Zinc metalloprotease ZmpB"
FT /id="PRO_0000026842"
FT TRANSMEM 77..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..1906
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REPEAT 277..291
FT /note="1-1"
FT REPEAT 293..315
FT /note="2-1"
FT REPEAT 361..375
FT /note="1-2"
FT REPEAT 380..402
FT /note="2-2"
FT REGION 178..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..375
FT /note="2 X 15 AA repeats of K-V-E-Q-A-G-E-P-V-A-P-R-E-D-E"
FT REGION 293..375
FT /note="2 X 23 AA approximate repeats"
FT MOTIF 73..77
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 178..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1563
FT /evidence="ECO:0000250"
FT BINDING 1562
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1586
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 76
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ 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
//
