IGA2_HAEIF
ID IGA2_HAEIF Reviewed; 1702 AA.
AC P45384;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Immunoglobulin A1 protease autotransporter;
DE EC=3.4.21.72;
DE Contains:
DE RecName: Full=Immunoglobulin A1 protease;
DE Short=IGA1 protease;
DE Contains:
DE RecName: Full=Immunoglobulin A1 protease translocator;
DE AltName: Full=Helper peptide;
DE Flags: Precursor;
GN Name=iga;
OS Haemophilus influenzae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=727;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HK715 / Serotype B;
RX PubMed=1373717; DOI=10.1128/jb.174.9.2913-2921.1992;
RA Poulsen K., Reinholdt J., Kilian M.;
RT "A comparative genetic study of serologically distinct Haemophilus
RT influenzae type 1 immunoglobulin A1 proteases.";
RL J. Bacteriol. 174:2913-2921(1992).
CC -!- FUNCTION: Virulence factor; cleaves host immunoglobulin A producing
CC intact Fc and Fab fragments.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of immunoglobulin A molecules at certain Pro-|-Xaa
CC bonds in the hinge region. No small molecule substrates are known.;
CC EC=3.4.21.72;
CC -!- SUBCELLULAR LOCATION: [Immunoglobulin A1 protease autotransporter]:
CC Periplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Immunoglobulin A1 protease]: Secreted. Cell
CC surface.
CC -!- SUBCELLULAR LOCATION: [Immunoglobulin A1 protease translocator]: Cell
CC outer membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Note=The cleaved C-terminal fragment (autotransporter
CC domain) is localized in the outer membrane. {ECO:0000250}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, insertion of
CC the C-terminal translocator domain in the outer membrane forms a
CC hydrophilic pore for the translocation of the passenger domain to the
CC bacterial cell surface, with subsequent cleavage (By similarity).
CC {ECO:0000250}.
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DR EMBL; M87489; AAA24966.1; -; Genomic_DNA.
DR PIR; A41859; A41859.
DR AlphaFoldDB; P45384; -.
DR SMR; P45384; -.
DR MEROPS; S06.007; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000710; Peptidase_S6.
DR InterPro; IPR030396; Peptidase_S6_dom.
DR InterPro; IPR004899; Pertactin_central.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF02395; Peptidase_S6; 1.
DR Pfam; PF03212; Pertactin; 1.
DR PRINTS; PR00921; IGASERPTASE.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51691; PEPTIDASE_S6; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Hydrolase; Membrane; Periplasm; Protease; Repeat;
KW Secreted; Serine protease; Signal; Transmembrane;
KW Transmembrane beta strand; Virulence; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1702
FT /note="Immunoglobulin A1 protease autotransporter"
FT /id="PRO_0000387600"
FT CHAIN 26..1014
FT /note="Immunoglobulin A1 protease"
FT /id="PRO_0000026962"
FT CHAIN 1015..1702
FT /note="Immunoglobulin A1 protease translocator"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026963"
FT DOMAIN 26..332
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT REPEAT 1109..1116
FT /note="1"
FT REPEAT 1117..1124
FT /note="2"
FT DOMAIN 1450..1702
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 991..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1124
FT /note="2 X 8 AA tandem repeats of A-K-V-E-K-E-E-K"
FT COMPBIAS 993..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1232..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 288
FT /evidence="ECO:0000305"
SQ SEQUENCE 1702 AA; 186539 MW; 860F70D2667807A6 CRC64;
MLNKKFKLNF IALTVAYALT PYTEAALVRD DVDYQIFRDF AENKGRFSVG ATNVEVRDKN
NHSLGNVLPN GIPMIDFSVV DVDKRIATLI NPQYVVGVKH VSNGVSELHF GNLNGNMNNG
NDKSHRDVSS EENRYFSVEK NEYPTKLNGK AVTTEDQTQK RREDYYMPRL DKFVTEVAPI
EASTASSDAG TYNDQNKYPA FVRLGSGSQF IYKKGDNYSL ILNNHEVGGN NLKLVGDAYT
YGIAGTPYKV NHENNGLIGF GNSKEEHSDP KGILSQDPLT NYAVLGDSGS PLFVYDREKG
KWLFLGSYDF WAGYNKKSWQ EWNIYKPEFA KTVLDKDTAG SLTGSNTQYN WNPTGKTSVI
SNGSESLNVD LFDSSQDTDS KKNNHGKSVT LRGSGTLTLN NNIDQGAGGL FFEGDYEVKG
TSDSTTWKGA GVSVADGKTV TWKVHNPKSD RLAKIGKGTL IVEGKGENKG SLKVGDGTVI
LKQQADANNK VKAFSQVGIV SGRSTVVLND DKQVDPNSIY FGFRGGRLDA NGNNLTFEHI
RNIDDGARLV NHNTSKTSTV TITGESLITD PNTITPYNID APDEDNPYAF RRIKDGGQLY
LNLENYTYYA LRKGASTRSE LPKNSGESNE NWLYMGKTSD EAKRNVMNHI NNERMNGFNG
YFGEEEGKNN GNLNVTFKGK SEQNRFLLTG GTNLNGDLKV EKGTLFLSGR PTPHARDIAG
ISSTKKDQHF AENNEVVVED DWINRNFKAT NINVTNNATL YSGRNVANIT SNITASDNAK
VHIGYKAGDT VCVRSDYTGY VTCTTDKLSD KALNSFNATN VSGNVNLSGN ANFVLGKANL
FGTISGTGNS QVRLTENSHW HLTGDSNVNQ LNLDKGHIHL NAQNDANKVT TYNTLTVNSL
SGNGSFYYLT DLSNKQGDKV VVTKSATGNF TLQVADKTGE PTKNELTLFD ASNATRNNLN
VSLVGNTVDL GAWKYKLRNV NGRYDLYNPE VEKRNQTVDT TNITTPNNIQ ADVPSVPSNN
EEIARVETPV PPPAPATPSE TTETVAENSK QESKTVEKNE QDATETTAQN GEVAEEAKPS
VKANTQTNEV AQSGSETEET QTTEIKETAK VEKEEKAKVE KEEKAKVEKD EIQEAPQMAS
ETSPKQAKPA PKEVSTDTKV EETQVQAQPQ TQSTTVAAAE ATSPNSKPAE ETQPSEKTNA
EPVTPVVSKN QTENTTDQPT EREKTAKVET EKTQEPPQVA SQASPKQEQS ETVQPQAVLE
SENVPTVNNA EEVQAQLQTQ TSATVSTKQP APENSINTGS ATAITETAEK SDKPQTETAA
STEDASQHKA NTVADNSVAN NSESSEPKSR RRRSISQPQE TSAEETTAAS TDETTIADNS
KRSKPNRRSR RSVRSEPTVT NGSDRSTVAL RDLTSTNTNA VISDAMAKAQ FVALNVGKAV
SQHISQLEMN NEGQYNVWVS NTSMNENYSS SQYRRFSSKS TQTQLGWDQT ISNNVQLGGV
FTYVRNSNNF DKASSKNTLA QVNFYSKYYA DNHWYLGIDL GYGKFQSNLK TNHNAKFARH
TAQFGLTAGK AFNLGNFGIT PIVGVRYSYL SNANFALAKD RIKVNPISVK TAFAQVDLSY
TYHLGEFSVT PILSARYDTN QGSGKINVNQ YDFAYNVENQ QQYNAGLKLK YHNVKLSLIG
GLTKAKQAEK QKTAELKLSF SF
