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   02-SEP-2026, entry version 125.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; 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: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:InterPro.
DR   GO; GO:0141140; P:symbiont-mediated suppression of host immunoglobulin-mediated immune response; EXP:SigSci.
DR   CDD; cd01343; PL1_Passenger_AT; 1.
DR   Gene3D; 2.160.20.20; -; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   Gene3D; 3.30.160.280; -; 1.
DR   Gene3D; 4.10.1240.40; -; 1.
DR   Gene3D; 2.40.128.130; Autotransporter beta-domain; 1.
DR   InterPro; IPR005546; Autotransporte_beta.
DR   InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR   InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR   InterPro; IPR050909; Bact_Autotransporter_VF.
DR   InterPro; IPR057069; IgA0_D2.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR000710; Peptidase_S6.
DR   InterPro; IPR030396; Peptidase_S6_dom.
DR   InterPro; IPR004899; Pertactin_central.
DR   InterPro; IPR057393; PIC_HAP1_IgA0_b-sol2.
DR   PANTHER; PTHR12338; AUTOTRANSPORTER; 1.
DR   PANTHER; PTHR12338:SF9; IMMUNOGLOBULIN A1 PROTEASE AUTOTRANSPORTER; 1.
DR   Pfam; PF03797; Autotransporter; 1.
DR   Pfam; PF24078; Beta-sol_PIC_HAP1_IgA0_2nd; 1.
DR   Pfam; PF24077; IgA0_D2; 1.
DR   Pfam; PF02395; Peptidase_S6; 1.
DR   Pfam; PF03212; Pertactin; 1.
DR   PRINTS; PR00921; IGASERPTASE.
DR   SMART; SM00869; Autotransporter; 1.
DR   SUPFAM; SSF103515; Autotransporter; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 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        997..1021
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1037..1047
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1049..1061
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1082..1095
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1104..1132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1150..1162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1163..1186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1207..1218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1219..1234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1235..1255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1263..1305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1316..1341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1360..1378
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1382..1392
FT                   /note="Basic 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
//