ID   IGA3_HAEIF              Reviewed;        1545 AA.
AC   P45385;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=HK393 / NCTC 8467 / ATCC 9795 / DSM 10001 / AMC 36-A-4 / 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; M87490; AAA24967.1; -; Genomic_DNA.
DR   PIR; B41859; B41859.
DR   AlphaFoldDB; P45385; -.
DR   SMR; P45385; -.
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..1545
FT                   /note="Immunoglobulin A1 protease autotransporter"
FT                   /id="PRO_0000387601"
FT   CHAIN           26..1012
FT                   /note="Immunoglobulin A1 protease"
FT                   /id="PRO_0000026964"
FT   CHAIN           1013..1545
FT                   /note="Immunoglobulin A1 protease translocator"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026965"
FT   DOMAIN          26..336
FT                   /note="Peptidase S6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT   DOMAIN          1293..1545
FT                   /note="Autotransporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT   REGION          995..1246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        995..1015
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1049..1077
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1078..1098
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1099..1124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1125..1220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        292
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1545 AA;  170627 MW;  3EDD753988F6D478 CRC64;
     MLNKKFKLNF IALTVAYALT PYTEAALVRD DVDYQIFRDF AENKGKFSVG ATNVEVRDKN
     NRPLGNVLPN GIPMIDFSVV DVDKRIATLV NPQYVVGVKH VSNGVSELHF GNLNGNMNNG
     NAKAHRDVSS EENRYYTVEK NEYPTKLNGK AVTTEDQAQK RREDYYMPRL DKFVTEVAPI
     EASTDSSTAG TYNNKDKYPY FVRLGSGTQF IYENGTRYEL WLGKEGQKSD AGGYNLKLVG
     NAYTYGIAGT PYEVNHENDG LIGFGNSNNE YINPKEILSK KPLTNYAVLG DSGSPLFVYD
     REKGKWLFLG SYDYWAGYNK KSWQEWNIYK PEFAEKIYEQ YSAGSLIGSK TDYSWSSNGK
     TSTITGGEKS LNVDLADGKD KPNHGKSVTF EGSGTLTLNN NIDQGAGGLF FEGDYEVKGT
     SDNTTWKGAG VSVAEGKTVT WKVHNPQYDR LAKIGKGTLI VEGTGDNKGS LKVGDGTVIL
     KQQTNGSGQH AFASVGIVSG RSTLVLNDDK QVDPNSIYFG FRGGRLDLNG NSLTFDHIRN
     IDEGARLVNH STSKHSTVTI TGDNLITDPN NVSIYYVKPL EDDNPYAIRQ IKYGYQLYFN
     EENRTYYALK KDASIRSEFP QNRGESNNSW LYMGTEKADA QKNAMNHINN ERMNGFNGYF
     GEEEGKNNGN LNVTFKGKSE QNRFLLTGGT NLNGDLNVQQ GTLFLSGRPT PHARDIAGIS
     STKKDSHFSE NNEVVVEDDW INRNFKATNI NVTNNATLYS GRNVESITSN ITASNNAKVH
     IGYKAGDTVC VRSDYTGYVT CTTDKLSDKA LNSFNPTNLR GNVNLTESAN FVLGKANLFG
     TIQSRGNSQV RLTENSHWHL TGNSDVHQLD LANGHIHLNS ADNSNNVTKY NTLTVNSLSG
     NGSFYYLTDL SNKQGDKVVV TKSATGNFTL QVADKTGEPN HNELTLFDAS KAQRDHLNVS
     LVGNTVDLGA WKYKLRNVNG RYDLYNPEVE KRNQTVDTTN ITTPNNIQAD VPSVPSNNEE
     IARVDEAPVP PPAPATPSET TETVAENSKQ ESKTVEKNEQ DATETTAQNR EVAKEAKSNV
     KANTQTNEVA QSGSETKETQ TTETKETATV EKEEKAKVET EKTQEVPKVT SQVSPKQEQS
     ETVQPQAEPA RENDPTVNIK EPQSQTNTTA DTEQPAKETS SNVEQPVTES TTVNTGNSVV
     ENPENTTPAT TQPTVNSESS NKPKNRHRRS VRSVPHNVEP ATTSSNDRST VALCDLTSTN
     TNAVLSDARA KAQFVALNVG KAVSQHISQL EMNNEGQYNV WVSNTSMNKN YSSSQYRRFS
     SKSTQTQLGW DQTISNNVQL GGVFTYVRNS NNFDKATSKN TLAQVNFYSK YYADNHWYLG
     IDLGYGKFQS KLQTNHNAKF ARHTAQFGLT AGKAFNLGNF GITPIVGVRY SYLSNADFAL
     DQARIKVNPI SVKTAFAQVD LSYTYHLGEF SVTPILSARY DANQGSGKIN VNGYDFAYNV
     ENQQQYNAGL KLKYHNVKLS LIGGLTKAKQ AEKQKTAELK LSFSF