IGA1B_STREE
ID IGA1B_STREE Reviewed; 1927 AA.
AC Q54875;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
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;
OS Streptococcus pneumoniae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=PK81 / Serotype 14;
RX PubMed=8926055; DOI=10.1128/iai.64.10.3957-3966.1996;
RA Poulsen K., Reinholdt J., Kilian M.;
RT "Characterization of the Streptococcus pneumoniae immunoglobulin A1
RT protease gene (iga) and its translation product.";
RL Infect. Immun. 64:3957-3966(1996).
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. May be responsible for
CC pneumococcal infection and is potentially involved in distinct stages
CC of pneumococcal disease. {ECO:0000269|PubMed:8926055}.
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; X94909; CAA64396.1; -; Genomic_DNA.
DR PDB; 6OH1; NMR; -; A=313-393.
DR PDBsum; 6OH1; -.
DR AlphaFoldDB; Q54875; -.
DR BMRB; Q54875; -.
DR SMR; Q54875; -.
DR MEROPS; M26.001; -.
DR PRIDE; Q54875; -.
DR BRENDA; 3.4.24.13; 1960.
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; IPR011493; GLUG.
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; PF07581; Glug; 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 1: Evidence at protein level;
KW 3D-structure; Cell wall; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Peptidoglycan-anchor; Protease; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix; Virulence; Zinc.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT PROPEP 43..99
FT /evidence="ECO:0000255"
FT /id="PRO_0000026835"
FT CHAIN 100..1927
FT /note="Immunoglobulin A1 protease"
FT /id="PRO_0000026836"
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..1927
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 235..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..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 426..640
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 371..385
FT /note="Polar 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..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 1565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1589
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"
FT STRAND 317..328
FT /evidence="ECO:0007829|PDB:6OH1"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:6OH1"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:6OH1"
FT STRAND 354..367
FT /evidence="ECO:0007829|PDB:6OH1"
FT STRAND 369..380
FT /evidence="ECO:0007829|PDB:6OH1"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:6OH1"
SQ SEQUENCE 1927 AA; 215172 MW; BAF74DB811301037 CRC64;
MEKYFGEKQE RFSFRKLSVG LVSATISSLF FMSVLASSSV DAQETAGVHY KYVADSELSS
EEKKQLVYDI PTYVENDDET YYLVYKLNSQ NQLAELPNTG SKNERQALVA GASLAALGIL
IFAVSKKKVK NKTVLHLVLV AGIGNGVLVS VHALENHLLL NYNTDYELTS GEKLPLPKEI
SGYTYIGYIK EGKTTSDFEV SNQEKSAATP TKQQKVDYNV TPNFVDHPST VQAIQEQTPV
SSTKPTEVQV VEKPFSTELI NPRKEEKQSS DSQEQLAEHK NLETKKEEKI SPKEKTGVNT
LNPQDEVLSG QLNKPELLYR EETIETKIDF QEEIQENPDL AEGTVRVKQE GKLGKKVEIV
RIFSVNKEEV SREIVSTSTT APSPRIVEKG TKKTQVIKEQ PETGVEHKDV QSGAIVEPAI
QPELPEAVVS DKGEPEVQPT LPEAVVTDKG EPAVQPELPE AVVSDKGEPE QVAPLPEYKG
NIEQVKPETP VEKTKEQGPE KTEEVPVKPT EETPVNPNEG TTEGTSIQGA ENPVQPAEDT
QTNSGKIANE NTGEVSNKPS DSKPPVEESN QPEKNGTATK PENSGNTTSE NGQTEPEPSN
GNSTEDVSTK SNTSNSNGNE EIKQENELDP DKKVEDPEKT LELRNVSDLE LYSLSNGTYK
QHISLEQVPS NPNSYFVKVK SSSFKDVYLP VASISEGRKN DKILYKITAK VEKLQQEIES
RYKDNFTFYL AKKGTEETTN FTSFSNLVKA INQNLSGTYH LGASLNANEV ELSTDDKSYI
KGTFTGQLIG EKDGKHYAIY NLKKPLFENL SGATVEKLSL KNVAISGKND IGSLANEATN
GTKIKQVHVD GVLAGERGVG GLLAKADQSS IAESSFKGRI VNTYETTDSY NIGGLVGHLT
GKNASIAKSK ATVTISSNTN RSDQTVGGLA GLVDRDAQIQ DSYAEGDINN VKHFGRVAGV
AGNLWDRTSG DVRHAGSLTN VLSDVNVTNG NAITGYHYTG MKVANTFSSK ANRVFNVTLE
KNEVVSKESF EERGTMLDAS QIASKKAEIN LITPPIVEPL STSGKKDSDF SKIAHYQANR
ALVYKNIEKL LPFYNKATIV KYGNLVKENS ILYQKELLSA VMMKDDQVIT DIISNKQTAN
KLLLHYKDHS SEKFDLRYQA DFANLAEYSI GDSGLLYTPN QFLYHQDSII NQVLPELNRV
NYQSDAVRNT LGISPEVKLT ELYLEEQFTK TKEHLAENLK KLLSSDAGLV TDNEVMTGYI
IDKIKRNKEA LLLGMSYLER WYNFSYGQVN VKDLVMYHPD FFGKGNTSPL DTLIELGKSG
FNNLLAKNNV DTYAISLASH HGTTDLFSTL ENYRKVFLPD KTNNDWFKSQ TKAYIVEEKS
NIEEVKTKQG LVGTKYSIGV YDRITSATWK YRNMVLPLLT LPERSVFVIS TISSLGFGAY
DRYRNKEHQA NGDLNSFVEK SAHETAERQR DHYDYWYRIL DEKGREKLYR NILLYDAYKF
GTNHTEGKAT EVADFDSPNP AMKHFFGPVG NKVGHNGHGA YATGDAVYYM GYRMLDKDGA
ITYTHEMTHN SDQDIYLGGY GRRSGLGPEF FAKGLLQAPD QPSDATITIN SILKHSKSDS
KEGERLQVLD PTTRFKDATD LQKYVHNMFD VVYMLEYLEG KSIVKKLNVY QKIEALRKIE
NQYLTDPADG NDVYATNVVK NLTEDEAKKL TSFDSLIDNN ILSAREYKAG TYERNGYFTI
KLFAPIFSAL SGEKGTPGDL MGRRIAFELL AAKGFKDGMV PYISNQYEED AKQQGQTINL
YGKERGLVTD ELVLKKVFDG KYKTWAEFKT AMYQERVDQF GNLKQVTFKD PTKPWPRYGT
KTINNVDELQ KLMDEAVLQD AKERNYYYWN NYNPETDSAV HKLKRAIFKA YLDQTNDFRR
SIFENKK
