IGA1_STRSA
ID IGA1_STRSA Reviewed; 1854 AA.
AC Q59986;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 92.
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 sanguinis.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 211-219, FUNCTION,
RP AND MUTAGENESIS OF HIS-1494 AND GLU-1495.
RC STRAIN=ATCC 10556 / DSM 20567 / JCM 5708 / LMG 14702 / NCIMB 702064 / NCTC
RC 7863;
RX PubMed=1987065; DOI=10.1128/iai.59.1.7-17.1991;
RA Gilbert J.V., Plaut A.G., Wright A.;
RT "Analysis of the immunoglobulin A protease gene of Streptococcus sanguis.";
RL Infect. Immun. 59:7-17(1991).
CC -!- FUNCTION: Zinc metalloproteinase which cleaves human immunoglobulin A1
CC (IgA1) in the hinge region. {ECO:0000269|PubMed:1987065}.
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 -!- ACTIVITY REGULATION: Inhibited by EDTA.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26901.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L29504; AAA26901.1; ALT_FRAME; Genomic_DNA.
DR PIR; A60272; A60272.
DR PIR; B60272; B60272.
DR AlphaFoldDB; Q59986; -.
DR SMR; Q59986; -.
DR MEROPS; M26.001; -.
DR PRIDE; Q59986; -.
DR BRENDA; 3.4.24.13; 5953.
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 Cell wall; Direct protein sequencing; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Peptidoglycan-anchor; Protease; Repeat; Secreted; Signal;
KW Transmembrane; Transmembrane helix; Zinc.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT PROPEP 38..99
FT /evidence="ECO:0000255"
FT /id="PRO_0000026839"
FT CHAIN 100..1854
FT /note="Immunoglobulin A1 protease"
FT /id="PRO_0000026840"
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..1854
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 256..335
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00437"
FT REPEAT 349..368
FT /note="1"
FT REPEAT 369..388
FT /note="2"
FT REPEAT 389..406
FT /note="3"
FT REPEAT 407..426
FT /note="4"
FT REPEAT 427..446
FT /note="5"
FT REPEAT 447..466
FT /note="6"
FT REPEAT 467..486
FT /note="7"
FT REPEAT 487..506
FT /note="8"
FT REPEAT 507..526
FT /note="9"
FT REPEAT 527..546
FT /note="10"
FT REGION 349..546
FT /note="10 X 20 AA approximate tandem repeats"
FT REGION 533..570
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 553..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1495
FT /evidence="ECO:0000305"
FT BINDING 1494
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
FT BINDING 1498
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1518
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 MUTAGEN 1494
FT /note="H->F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1987065"
FT MUTAGEN 1495
FT /note="E->K: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1987065"
SQ SEQUENCE 1854 AA; 206024 MW; CE2149C0BC7FA4DE CRC64;
MKKFLGEKQT RFAFRKLAVG LVSAAISSLF FVSIVGVDSV QAQEKLNVHY KYVTDTEITP
QEKELIVSGV PRMPEGNEET YYLVYRLNSN AGAKTLPNTG DNNSNTMMAA GLLLTTIGLV
VFAVSKRKVQ SKFLLTVLVG ASVGGGLILS VDALENGSLL QYNAEYQVSA GESLPSPGEI
SGYTYVGYIK DESIKKLLDN KIPDNQQNAN VDKEALNQNK KLDYSVSFDK NGLKNQTVGV
NTIEPQDEVL SGRVAKPELL YKETSIETEI AYGEQIQENP DLAEGTVRVK QEGKPGRKIE
VVRIFTVDNA EVSREVLSTK IEEATPKIVE KGTKKLEAPS EKPVTSNLVQ PEQVAPLPEY
TGVQSGAIVE PEQVASLPEY SGTLSGAIVE PEQIEPEIGG VQSGAIVEPE QVTPLPEYTG
TQAGAVVSPE QVAPLPEYTG TQSGAIVEPA QVTPLPEYTG VQSGAIVKPA QVTPLPEYTG
TQSGAIVEPE QVTPSPEYTG VQAGAIVEPE QVASLPEYTG SQAGAIVEPE QVEPPQEYTG
NIEPAAPEAE NPTEKAQEPK EQKQEPEKNI ELRNVSDVEL YSLADGKYKQ HVSLDAIPSN
QENYFVKVKS SKFKDVFLPI SSIVDSTKDG QPVYKITASA EKLKQDVNNK YEDNFTFYLA
KKAEREVTNF TSFSNLVQAI NNNLNGTYYL AASLNANEVE LENGASSYIK GRFTGKLFGS
KDGKNYAIYN LKKPLFDTLS AATVENLTLK DVNISGKTDI GALANEANNA TRINNVHVDG
VLAGERGIGG LVWKADNSKI SNSSFKGRIV NSYETKAPYN IGGLVGQLTG INALVDKSKA
TITISSNADS TNQTVGGLAG LVEKDALISN SYAEGNINNV KRFGSVAGVA GYLWDRDSSE
ERHAGRLHNV LSDINVMNGN AISGYHYRGM RITDSYSNKD NRVYKVTLEK DEVVTKESLE
ERGTILDVSQ IASKKSEINS LSAPKVETLL TSTNKESDFS KVKDYQASRA LAYKNIEKLL
PFYNKATIVK YGNLVKEDST LYEKEILSAV MMKDNEVITD IASHKEAANK LLIHYKDHSS
EKLDLTYQSD FSKLAEYRVG DTGLIYTPNQ FLQNHSSIVN EVLPDLKAVD YQSEAIRNTL
GISSGVSLTE LYLEEQFAKT KENLANTLEK LLSADAVIAS ENQTINGYVV DKIKRNKEAL
LLGLTYLERW YNFNYGDVNV KDLVMYHMDF FGKGNVSPLD TIIELGKSGF NNLLAKNNVD
AYNISLANNN ATKDLFSTLA NYREVFLPNK TNNQWFKEQT KAYIVEEKSA IDEVRVKQEQ
AGSKYSIGVY DRITSDTWKY RNMVLPLLTM PERSVFVIST ISSLGFGAYD RYRNNEHRAG
AELNKFVEDN AQETAKRQRD HYDYWYRILD EQGREKLYRN ILVYDAYKFG DDTTVDKATV
EAQFDSSNPA MKYFFGPVGN KVVHNKHGAY ATGDSVYYMG YRMLDKDGAI TYTHEMTHDS
DNEIYLGGYG RRSGLGPEFF AKGLLQAPDH PDDATITVNS ILKYDKNDAS EKSRLQVLDP
TKRFQNADDL KNYVHNMFDV IYMLEYLEGM SIVNRLSDVQ KVNALRKIEN KYVRDADGND
VYATNVIKNI TMADAQKLNS FNSLIENDIL SAREYKNGDV ERNGYHTIKL FSPIYSALSS
EKGTPGDLMG RRIAYELLAA KGFKDGMVPY ISNQYEDDAK QNGKTISIYG KTRGLVTDDL
VLRKVFNGQF NNWTEFKKAM YEERKNKFDS LNKVTFDDTR QPWTSYATKT ISTVEELQTL
MDEAVLQDAN DNWYSWSGYK PEYNSAVHKL KKAVFKAYLD QTKDFRKSIF ENQK
