IGA1_STRR6
ID IGA1_STRR6 Reviewed; 1963 AA.
AC Q59947; Q8DPR5;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 118.
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=spr1042;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CELL SURFACE LOCALIZATION.
RX PubMed=8926056; DOI=10.1128/iai.64.10.3967-3974.1996;
RA Wani J.H., Gilbert J.V., Plaut A.G., Weiser J.N.;
RT "Identification, cloning and sequencing of the immunoglobulin A1 protease
RT gene of Streptococcus pneumoniae.";
RL Infect. Immun. 64:3967-3974(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
CC -!- FUNCTION: Zinc metalloproteinase which cleaves human immunoglobulin A1
CC (IgA1) in the hinge region. {ECO:0000269|PubMed:8926056}.
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. 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}.
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DR EMBL; U47687; AAC44568.1; -; Genomic_DNA.
DR EMBL; AE007317; AAK99846.1; -; Genomic_DNA.
DR PIR; B98002; B98002.
DR RefSeq; NP_358636.1; NC_003098.1.
DR RefSeq; WP_000417171.1; NC_003098.1.
DR PDB; 6XJA; EM; 4.00 A; P=665-1963.
DR PDB; 6XJB; EM; 3.80 A; A=674-1958.
DR PDB; 7JGJ; EM; 4.80 A; A=674-1963.
DR PDBsum; 6XJA; -.
DR PDBsum; 6XJB; -.
DR PDBsum; 7JGJ; -.
DR AlphaFoldDB; Q59947; -.
DR SMR; Q59947; -.
DR STRING; 171101.spr1042; -.
DR MEROPS; M26.001; -.
DR PRIDE; Q59947; -.
DR EnsemblBacteria; AAK99846; AAK99846; spr1042.
DR GeneID; 60233287; -.
DR KEGG; spr:spr1042; -.
DR PATRIC; fig|171101.6.peg.1133; -.
DR eggNOG; COG0810; Bacteria.
DR eggNOG; COG3583; Bacteria.
DR HOGENOM; CLU_000802_0_0_9; -.
DR OMA; KEYTGVQ; -.
DR BRENDA; 3.4.24.13; 1960.
DR Proteomes; UP000000586; 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; 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; 2.
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; Reference proteome;
KW Repeat; Secreted; Signal; Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..36
FT /evidence="ECO:0000255"
FT PROPEP 37..99
FT /evidence="ECO:0000255"
FT /id="PRO_0000026837"
FT CHAIN 100..1963
FT /note="Immunoglobulin A1 protease"
FT /id="PRO_0000026838"
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..1963
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 253..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..469
FT /note="3 X 17 AA approximate tandem repeats"
FT MOTIF 96..100
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
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..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1605
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 1604
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1608
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1628
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 CONFLICT 766
FT /note="T -> S (in Ref. 1; AAC44568)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="N -> I (in Ref. 1; AAC44568)"
FT /evidence="ECO:0000305"
FT CONFLICT 1205
FT /note="A -> P (in Ref. 1; AAC44568)"
FT /evidence="ECO:0000305"
FT CONFLICT 1520..1532
FT /note="DEQSREKLYRTIL -> VNSQRRKTLFVRFS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 1601
FT /note="T -> N (in Ref. 1; AAC44568)"
FT /evidence="ECO:0000305"
FT CONFLICT 1650
FT /note="S -> F (in Ref. 1; AAC44568)"
FT /evidence="ECO:0000305"
FT CONFLICT 1680
FT /note="L -> F (in Ref. 1; AAC44568)"
FT /evidence="ECO:0000305"
FT CONFLICT 1876..1879
FT /note="VDQF -> WISL (in Ref. 1; AAC44568)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1963 AA; 218571 MW; AA409DFF3D548F7D CRC64;
MEKYFGEKQE RFSFRKLSVG LVSATISSLF FMSVLASSSV DAQETAGVHY KYVADSELSS
EEKKQLVYDI PTYVENDDET YYLVYKLNSQ NQLAELPNTG SKNERQALVA GASLAALGIL
IFAVSKKKVK NKTVLHLVLV AGMGNGVLVS 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 ETEVQPESPD TVVSDKGEPE QVAPLPEYKG
NIEQVKPETP VEKTKEQGPE KTEEVPVKPT EETPVNPNEG TTEGTSIQEA ENPVQPAEES
TTNSEKVSPD TSSENTGEVS SNPSDSTTSV GESNKPEHND SKNENSEKTV EEVPVNPNEG
TVEGTSNQET EKPVQPAEET QTNSGKIANE NTGEVSNKPS DSKPPVEESN QPEKNGTATK
PENSGNTTSE NGQTEPEKKL ELRNVSDIEL YSQTNGTYRQ HVSLDGIPEN TDTYFVKVKS
SAFKDVYIPV ASITEEKRNG QSVYKITAKA EKLQQELENK YVDNFTFYLD KKAKEENTNF
TSFSNLVKAI NQNPSGTYHL AASLNANEVE LGPDERSYIK DTFTGRLIGE KDGKNYAIYN
LKKPLFENLS GATVEKLSLK NVAISGKNDI GSLANEATNG TKIKQVHVDG VLAGERGVGG
LLAKADQSSI AESSFKGRIV NTYETTDAYN IGGLVGHLTG KNASIAKSKA TVTISSNTNR
SDQTVGGLAG LVDQDAHIQN SYAEGDINNV KHFGKVAGVA GYLWDRTSGE EKHAGELTNV
LSDVNVTNGN AITGYHYTGM KVANTFSSKA NRVFNVTLEK DEVVSKESFE ERGTMLDASQ
IVSKKAEINP LTLPTVEPLS TSGKKDSDFS KIAHYQANRA LVYKNIEKLL PFYNKSTIVK
YGNLVKENSL LYQKELLSAV MMKDDQVITD IVSNKQTANK LLLHYNDHSS EKFDLKYQTD
FANLAEYNLG NTGLLYTPNQ FLYDRDSIVK EVLPELQKLD YQSDAIRKTL GISPEVKLTE
LYLEDQFSKT KQNLGDSLKK LLSADAGLAS DNSVTRGYLV DKIKNNKEAL LLGLTYLERW
YNFNYGQVNV KDLVMYHPDF FGKGNTSPLD TLIELGKSGF NNLLAKNNVD TYGISLASQH
GATDLFSTLE HYRKVFLPNT SNNDWFKSET KAYIVEEKST IEEVKTKQGL AGTKYSIGVY
DRITSATWKY RNMVLPLLTL PERSVFVIST MSSLGFGAYD RYRSSDHKAG KALNDFVEEN
ARETAKRQRD HYDYWYRILD EQSREKLYRT ILLYDAYKFG DDTTSGKATA EAKFDSSNPA
MKNFFGPVGN KVVHNQHGAY ATGDGVYYMS YRMLDKDGAI TYTHEMTHDS DQDIYLGGYG
RRNGLGPEFF AKGLLQAPDQ PSDATITINS ILKHSKSDST EGSRLQVLDP TERFQNAADL
QNYVHNMFDL IYMMEYLEGQ SIVNKLSVYQ KMAALRKIEN KYVKDPADGN EVYATNVVKE
LTEAEARNLN SFESLIDHNI LSAREYQSGD YERNGYYTIK LFAPIYSALS SEKGTPGDLM
GRRIAYELLA AKGFKDGMVP YISNQYEEDA KQQGQTINLY GKERGLVTDE LVLKKVFDGK
YKTWAEFKTA MYQERVDQFG NLKQVTFKDP TKPWPSYGTK TINNVDELQA LMDQAVLKDA
EGPRWSNYDP EIDSAVHKLK RAIFKAYLDQ TNDFRSSIFE NKK
