IGA1_HAEIF
ID IGA1_HAEIF Reviewed; 1541 AA.
AC P42782;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=HK368 / Serotype B;
RX PubMed=2506130; DOI=10.1128/iai.57.10.3097-3105.1989;
RA Poulsen K., Brandt J., Hjorth J.P., Thoegersen H.C., Kilian M.;
RT "Cloning and sequencing of the immunoglobulin A1 protease gene (iga) of
RT Haemophilus influenzae serotype b.";
RL Infect. Immun. 57:3097-3105(1989).
RN [2]
RP MUTAGENESIS OF SER-288.
RC STRAIN=HK368 / 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; X64357; CAA45708.1; -; Genomic_DNA.
DR EMBL; M87492; AAA24969.1; -; Genomic_DNA.
DR PIR; A37023; A37023.
DR AlphaFoldDB; P42782; -.
DR SMR; P42782; -.
DR MEROPS; S06.007; -.
DR PRIDE; P42782; -.
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 1: Evidence at protein level;
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..1541
FT /note="Immunoglobulin A1 protease autotransporter"
FT /id="PRO_0000387599"
FT CHAIN 26..1008
FT /note="Immunoglobulin A1 protease"
FT /id="PRO_0000026960"
FT CHAIN 1009..1541
FT /note="Immunoglobulin A1 protease translocator"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026961"
FT DOMAIN 26..332
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1289..1541
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 991..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1094
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 288
FT /evidence="ECO:0000305"
FT MUTAGEN 288
FT /note="S->T: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1373717"
SQ SEQUENCE 1541 AA; 169369 MW; CE7257CB3196C600 CRC64;
MLNKKFKLNF IALTVAYALT PYTEAALVRD DVDYQIFRDF AENKGKFSVG ATNVLVKDKN
NKDLGTALPN GIPMIDFSVV DVDKRIATLI NPQYVVGVKH VSNGVSELHF GNLNGNMNNG
NAKAHRDVSS EENRYFSVEK NEYPTKLNGK TVTTEDQTQK RREDYYMPRL DKFVTEVAPI
EASTASSDAG TYNDQNKYPA FVRLGSGSQF IYKKGDNYSL ILNNHEVGGN NLKLVGDAYT
YGIAGTPYKV NHENNGLIGF GNSKEEHSDP KGILSQDPLT NYAVLGDSGS PLFVYDREKG
KWLFLGSYDF WAGYNKKSWQ EWNIYKSQFT KDVLNKDSAG SLIGSKTDYS WSSNGKTSTI
TGGEKSLNVD LADGKDKPNH GKSVTFEGSG TLTLNNNIDQ GAGGLFFEGD YEVKGTSDNT
TWKGAGVSVA EGKTVTWKVH NPQYDRLAKI GKGTLIVEGT GDNKGSLKVG DGTVILKQQT
NGSGQHAFAS VGIVSGRSTL VLNDDKQVDP NSIYFGFRGG RLDLNGNSLT FDHIRNIDDG
ARLVNHNMTN ASNITITGES LITDPNTITP YNIDAPDEDN PYAFRRIKDG GQLYLNLENY
TYYALRKGAS TRSELPKNSG ESNENWLYMG KTSDEAKRNV MNHINNERMN GFNGYFGEEE
GKNNGNLNVT FKGKSEQNRF LLTGGTNLNG DLTVEKGTLF LSGRPTPHAR DIAGISSTKK
DPHFAENNEV VVEDDWINRN FKATTMNVTG NASLYSGRNV ANITSNITAS NKAQVHIGYK
TGDTVCVRSD YTGYVTCTTD KLSDKALNSF NPTNLRGNVN LTESANFVLG KANLFGTIQS
RGNSQVRLTE NSHWHLTGNS DVHQLDLANG HIHLNSADNS NNVTKYNTLT VNSLSGNGSF
YYLTDLSNKQ GDKVVVTKSA TGNFTLQVAD KTGEPNHNEL TLFDASKAQR DHLNVSLVGN
TVDLGAWKYK LRNVNGRYDL YNPEVEKRNQ TVDTTNITTP NNIQADVPSV PSNNEEIARV
DEAPVPPPAP ATPSETTETV AENSKQESKT VEKNEQDATE TTAQNREVAK EAKSNVKANT
QTNEVAQSGS ETKETQTTET KETATVEKEE KAKVETEKTQ EVPKVTSQVS PKQEQSETVQ
PQAEPAREND PTVNIKEPQS QTNTTADTEQ PAKETSSNVE QPVTESTTVN TGNSVVENPE
NTTPATTQPT VNSESSNKPK NRHRRSVRSV PHNVEPATTS SNDRSTVALC DLTSTNTNAV
LSDARAKAQF VALNVGKAVS QHISQLEMNN EGQYNVWVSN TSMNKNYSSS QYRRFSSKST
QTQLGWDQTI SNNVQLGGVF TYVRNSNNFD KATSKNTLAQ VNFYSKYYAD NHWYLGIDLG
YGKFQSKLQT NHNAKFARHT AQFGLTAGKA FNLGNFGITP IVGVRYSYLS NADFALDQAR
IKVNPISVKT AFAQVDLSYT YHLGEFSVTP ILSARYDANQ GSGKINVNGY DFAYNVENQQ
QYNAGLKLKY HNVKLSLIGG LTKAKQAEKQ KTAELKLSFS F
