IGA1A_STRPN
ID IGA1A_STRPN Reviewed; 2004 AA.
AC Q97QP7;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Immunoglobulin A1 protease;
DE Short=IgA1 protease;
DE EC=3.4.24.13;
DE AltName: Full=IgA-specific zinc metalloproteinase;
DE Flags: Precursor;
GN Name=iga; OrderedLocusNames=SP_1154;
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).
CC -!- FUNCTION: Zinc metalloproteinase which cleaves human immunoglobulin A1
CC (IgA1) in the hinge region, rendering it less efficient in coating the
CC surface of colonizing or invading pneumococci. Strongly contributes to
CC virulence in mice. May be responsible for pneumococcal infection and is
CC potentially involved in distinct stages of pneumococcal disease.
CC {ECO:0000269|PubMed:12841855}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of Pro-|-Thr bond in the hinge region of the heavy
CC chain of human IgA.; EC=3.4.24.13;
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:0000255|PROSITE-
CC ProRule:PRU00477}. Membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00477}.
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; AAK75263.1; -; Genomic_DNA.
DR PIR; F95133; F95133.
DR RefSeq; WP_000417180.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97QP7; -.
DR SMR; Q97QP7; -.
DR STRING; 170187.SP_1154; -.
DR MEROPS; M26.001; -.
DR PRIDE; Q97QP7; -.
DR EnsemblBacteria; AAK75263; AAK75263; SP_1154.
DR KEGG; spn:SP_1154; -.
DR eggNOG; COG0810; Bacteria.
DR eggNOG; COG3583; Bacteria.
DR OMA; KEYTGVQ; -.
DR PhylomeDB; Q97QP7; -.
DR BioCyc; SPNE170187:G1FZB-1174-MON; -.
DR BRENDA; 3.4.24.13; 1960.
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; PF00746; Gram_pos_anchor; 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; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix; Virulence; Zinc.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT PROPEP 43..99
FT /evidence="ECO:0000255"
FT /id="PRO_0000026833"
FT CHAIN 100..2004
FT /note="Immunoglobulin A1 protease"
FT /id="PRO_0000026834"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..2004
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 314..393
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT REPEAT 419..435
FT /note="1"
FT REPEAT 436..452
FT /note="2"
FT REPEAT 453..469
FT /note="3"
FT REGION 194..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..469
FT /note="3 X 17 AA approximate tandem repeats"
FT REGION 422..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 96..100
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 235..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1646
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 1645
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1649
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 99
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 2004 AA; 223909 MW; 556BC6A1028D60A4 CRC64;
MEKYFGEKQE RFSFRKLSVG LVSATISSLF FMSVLASSSV DAQETAGVHY KYVADSELSS
EEKKQLVYDI PTYVENDDET YYLVYKLNSQ NQLAELPNTG SKNERQALVA GASLAAMGIL
IFAVSKKKVK NKTVLHLVLV AGIGNGVLVS VHALENHLLL NYNTDYELTS GEKLPLPKEI
SGYTYIGYIK EGKTTSESEV SNQKSSVATP TKQQKVDYNV TPNFVDHPST VQAIQEQTPV
SSTKPTEVQV VEKPFSTELI NPRKEEKQSS DSQEQLAEHK NLETKKEEKI SPKEKTGVNT
LNPQDEVLSG QLNKPELLYR EETMETKIDF QEEIQENPDL AEGTVRVKQE GKLGKKVEIV
RIFSVNKEEV SREIVSTSTT APSPRIVEKG TKKTQVIKEQ PETGVEHKDV QSGAIVEPAI
QPELPEAVVS DKGEPEVQPT LPEAVVTDKG ETEVQPESPD TVVSDKGEPE QVAPLPEYKG
NIEQVKPETP VEKTKEQGPE KTEEVPVKPT EETPVNPNEG TTEGTSIQEA ENPVQPAEES
TTNSEKVSPD TSSKNTGEVS SNPSDSTTSV GESNKPEHND SKNENSEKTV EEVPVNPNEG
TVEGTSNQET EKPVQPAEET QTNSGKIANE NTGEVSNKPS DSKPPVEESN QPEKNGTATK
PENSGNTTSE NGQTEPEPSN GNSTEDVSTE SNTSNSNGNE EIKQENELDP DKKVEEPEKT
LELRNVSDLE LYSLSNGTYK QHISLEQVPS NPNSYFVKVK SSSFKDVYLP VASISEERKN
DKILYKITAK VEKLQQEIES RYKDNFTFYL AKKGTEETTN FTSFSNLVKA INQNPSGTYH
LAASLNANEV ELGPDERSYI KDTFTGRLIG EKDGKNYAIY NLKKPLFENL SGATVEKLSL
KNVAISGKDD IGSLANEAQN NTKIKQVHVD GVLAGERGIG GLLAKAEQSS ITESSFKGRI
INTYETTAAY NIGGMVGHLT GDKALLTKSK ATVAISSNTN TSDQTVGGLA GLVDRDAQIQ
DSYAEGDINN VKHFGRVAGV AGNLWDRTSG DVRHAGSLTN VLSDVNVTNG NAITGYHYNE
MKVKDTFSSK ANRVYNVTLV KDEVVSKESF EERGTMLDAS QIASKKAEIN PLILPTVEPL
STSGKKDSDF SKVAYYQAKR NLTYKNIEKL LPFYNKATIV KYGNLVNENS LLYQKELLSA
VMMKDNQVIT DIVSNKQTAN KLLLHYKDDL SEKLDLKYQN DFAKLAEYSL GNTGLLYTPN
QFLYDQTSII KQVLPDLQKV DYHSEAIRKT LGISPNVKQT ELYLEDQFAK TKQQLEDSLK
KLLSADAGLA SANPVTEGYL VDKIKRNKEA LLLGLTYLER WYNFSYGQVN VKDLVLYHLD
FFGKGNASPL DTLIELGKSG FNNLLAKNNV DTYGISLASQ HGTTDLFSTL EHYRKVFLPN
TSNNDWFKSE TKAYIVEEKS TIEEVKTKQG LAGTKYSIGV YDRITSATWK YRNMVLPLLT
LPERSVFVIS TMSSLGFGAY DRYRSSDHKA GKALNDFVEE NARETAKRQR DHYDYWYRIL
DDNAREKLYR NILLYDAYKF GDDNTVGKAT EVADFDNPNP AMQHFFGPVG NKVGHNQHGA
YATGDAVYYM GYRMLDKDGA ITYTHEMTHD SDQDIYLGGY GRRSGLGPEF FAKGLLQAPD
HPDDATITIN SILKHSKSDS TESRRLQVLD PTTRFNNADD LKQYVHNMFD VVYMLEYLEG
NSILKLDTNQ KQQLLRKVTN EYHPDPDGNK VYATNVVRNL TVEEVERLRS FNDLIDNNIL
SSREYASGKY ERNGYFTIKL FAPIYAALSN DIGTPGDLMG RRIAYELLAA KGFKDGMVPY
ISNQYEEEAK QKGKTINLYG KTRGLVTDDL VLEKVFNNQY HTWSEFKKAM YQERQDQFDR
LNKVTFNDTT QPWQTFAKKT TSSVDELQKL MDVAVRKDAE HNYYHWNNYN PDIDSEVHKL
KRAIFKAYLD QTNDFRSSIF ENKK
