ID   IGA4_HAEIF              Reviewed;        1849 AA.
AC   P45386;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=NHTI HK61;
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; M87491; AAA24968.1; -; Genomic_DNA.
DR   PIR; C41859; C41859.
DR   AlphaFoldDB; P45386; -.
DR   SMR; P45386; -.
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; Secreted;
KW   Serine protease; Signal; Transmembrane; Transmembrane beta strand;
KW   Virulence; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..1849
FT                   /note="Immunoglobulin A1 protease autotransporter"
FT                   /id="PRO_0000387602"
FT   CHAIN           26..1021
FT                   /note="Immunoglobulin A1 protease"
FT                   /id="PRO_0000026966"
FT   CHAIN           1022..1849
FT                   /note="Immunoglobulin A1 protease translocator"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026967"
FT   DOMAIN          26..343
FT                   /note="Peptidase S6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT   DOMAIN          1597..1849
FT                   /note="Autotransporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT   REGION          998..1538
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1000..1031
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1163..1184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1185..1203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1232..1289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1304..1440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1452..1473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1474..1488
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1489..1512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1521..1538
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        299
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1849 AA;  202957 MW;  79A7D018C7150AEA CRC64;
     MLNKKFKLNF IALTVAYALT PYTEAALVRD DVDYQIFRDF AENKGKFSVG ATNVEVRDKK
     NQSLGSALPN GIPMIDFSVV DVDKRIATLV NPQYVVGVKH VSNGVSELHF GNLNGNMNNG
     NAKSHRDVSS EENRYYTVEK NNFPTENVTS FTTKEEQDAQ KRREDYYMPR LDKFVTEVAP
     IEASTANNNK GEYNNSDKYP AFVRLGSGSQ FIYKKGSRYQ LILTEKDKQG NLLRNWDVGG
     DNLELVGNAY TYGIAGTPYK VNHENNGLIG FGNSKEEHSD PKGILSQDPL TNYAVLGDSG
     SPLFVYDREK GKWLFLGSYD FWAGYNKKSW QEWNIYKHEF AEKIYQQYSA GSLTGSNTQY
     TWQATGSTST ITGGGEPLSV DLTDGKDKPN HGKSITLKGS GTLTLNNHID QGAGGLFFEG
     DYEVKGTSDS TTWKGAGVSV ADGKTVTWKV HNPKYDRLAK IGKGTLVVEG KGKNEGLLKV
     GDGTVILKQK ADANNKVQAF SQVGIVSGRS TLVLNDDKQV DPNSIYFGFR GGRLDLNGNS
     LTFDHIRNID DGARVVNHNM TNTSNITITG ESLITNPNTI TSYNIEAQDD DHPLRIRSIP
     YRQLYFNQDN RSYYTLKKGA STRSELPQNS GESNENWLYM GRTSDEAKRN VMNHINNERM
     NGFNGYFGEE ETKATQNGKL NVTFNGKSDQ NRFLLTGGTN LNGDLNVEKG TLFLSGRPTP
     HARDIAGISS TKKDPHFTEN NEVVVEDDWI NRNFKATTMN VTGNASLYSG RNVANITSNI
     TASNNAQVHI GYKTGDTVCV RSDYTGYVTC HNSNLSEKAL NSFNPTNLRG NVNLTENASF
     TLGKANLFGT IQSIGTSQVN LKENSHWHLT GNSNVNQLNL TNGHIHLNAQ NDANKVTTYN
     TLTVNSLSGN GSFYYWVDFT NNKSNKVVVN KSATGNFTLQ VADKTGEPNH NELTLFDASN
     ATRNNLEVTL ANGSVDRGAW KYKLRNVNGR YDLYNPEVEK RNQTVDTTNI TTPNDIQADA
     PSAQSNNEEI ARVETPVPPP APATESAIAS EQPETRPAET AQPAMEETNT ANSTETAPKS
     DTATQTENPN SESVPSETTE KVAENPPQEN ETVAKNEQEA TEPTPQNGEV AKEDQPTVEA
     NTQTNEATQS EGKTEETQTA ETKSEPTESV TVSENQPEKT VSQSTEDKVV VEKEEKAKVE
     TEETQKAPQV TSKEPPKQAE PAPEEVPTDT NAEEAQALQQ TQPTTVAAAE TTSPNSKPAE
     ETQQPSEKTN AEPVTPVVSE NTATQPTETE ETAKVEKEKT QEVPQVASQE SPKQEQPAAK
     PQAQTKPQAE PARENVLTTK NVGEPQPQAQ PQTQSTAVPT TGETAANSKP AAKPQAQAKP
     QTEPARENVS TVNTKEPQSQ TSATVSTEQP AKETSSNVEQ PAPENSINTG SATTMTETAE
     KSDKPQMETV TENDRQPEAN TVADNSVANN SESSESKSRR RRSVSQPKET SAEETTVAST
     QETTVDNSVS TPKPRSRRTR RSVQTNSYEP VELPTENAEN AENVQSGNNV ANSQPALRNL
     TSKNTNAVLS NAMAKAQFVA LNVGKAVSQH ISQLEMNNEG QYNVWISNTS MNKNYSSEQY
     RRFSSKSTQT QLGWDQTISN NVQLGGVFTY VRNSNNFDKA SSKNTLAQVN FYSKYYADNH
     WYLGIDLGYG KFQSNLQTNN NAKFARHTAQ IGLTAGKAFN LGNFAVKPTV GVRYSYLSNA
     DFALAQDRIK VNPISVKTAF AQVDLSYTYH LGEFSITPIL SARYDANQGN GKINVSVYDF
     AYNVENQQQY NAGLKLKYHN VKLSLIGGLT KAKQAEKQKT AEVKLSFSF