IGA0_HAEIN
ID IGA0_HAEIN Reviewed; 1694 AA.
AC P44969;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
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; Synonyms=iga1; OrderedLocusNames=HI_0990;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype D;
RA Wright A., Fishman Y., Tai F., Plaut A.G.;
RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [3]
RP CHARACTERIZATION OF CLEAVAGE SITE SPECIFICITY.
RX PubMed=2105270; DOI=10.1128/iai.58.2.320-331.1990;
RA Grundy F.J., Plaut A.G., Wright A.;
RT "Localization of the cleavage site specificity determinant of Haemophilus
RT influenzae immunoglobulin A1 protease genes.";
RL Infect. Immun. 58:320-331(1990).
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; X59800; CAB56789.1; -; Genomic_DNA.
DR EMBL; L42023; AAC22651.1; -; Genomic_DNA.
DR PIR; H64106; H64106.
DR RefSeq; NP_439153.1; NC_000907.1.
DR RefSeq; WP_005693332.1; NC_000907.1.
DR PDB; 3H09; X-ray; 1.75 A; A/B=26-1014.
DR PDBsum; 3H09; -.
DR AlphaFoldDB; P44969; -.
DR SMR; P44969; -.
DR STRING; 71421.HI_0990; -.
DR BindingDB; P44969; -.
DR ChEMBL; CHEMBL4739848; -.
DR MEROPS; S06.007; -.
DR EnsemblBacteria; AAC22651; AAC22651; HI_0990.
DR KEGG; hin:HI_0990; -.
DR PATRIC; fig|71421.8.peg.1033; -.
DR eggNOG; COG3266; Bacteria.
DR eggNOG; COG3468; Bacteria.
DR HOGENOM; CLU_004023_0_0_6; -.
DR OMA; AAPQDYM; -.
DR BioCyc; HINF71421:G1GJ1-1032-MON; -.
DR BRENDA; 3.4.21.72; 2529.
DR EvolutionaryTrace; P44969; -.
DR Proteomes; UP000000579; Chromosome.
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 3D-structure; Cell outer membrane; Hydrolase; Membrane; Periplasm;
KW Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Transmembrane; Transmembrane beta strand; Virulence; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1694
FT /note="Immunoglobulin A1 protease autotransporter"
FT /id="PRO_0000387598"
FT CHAIN 26..1014
FT /note="Immunoglobulin A1 protease"
FT /id="PRO_0000026958"
FT CHAIN 1015..1694
FT /note="Immunoglobulin A1 protease translocator"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026959"
FT DOMAIN 26..332
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1442..1694
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 991..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 288
FT /evidence="ECO:0000305"
FT CONFLICT 253..254
FT /note="EN -> GV (in Ref. 1; CAB56789)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="G -> A (in Ref. 1; CAB56789)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="G -> E (in Ref. 1; CAB56789)"
FT /evidence="ECO:0000305"
FT CONFLICT 866
FT /note="S -> T (in Ref. 1; CAB56789)"
FT /evidence="ECO:0000305"
FT CONFLICT 1036
FT /note="A -> D (in Ref. 1; CAB56789)"
FT /evidence="ECO:0000305"
FT CONFLICT 1074
FT /note="A -> G (in Ref. 1; CAB56789)"
FT /evidence="ECO:0000305"
FT CONFLICT 1421
FT /note="A -> G (in Ref. 1; CAB56789)"
FT /evidence="ECO:0000305"
FT CONFLICT 1545
FT /note="H -> T (in Ref. 1; CAB56789)"
FT /evidence="ECO:0000305"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 34..42
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3H09"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:3H09"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 207..218
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:3H09"
FT TURN 297..300
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 301..311
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 327..337
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 338..354
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 365..368
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 379..384
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 388..401
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 410..412
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 414..422
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 451..462
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 497..499
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 504..510
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 535..538
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 547..550
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 558..562
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:3H09"
FT TURN 603..606
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 607..611
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 630..638
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 639..653
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 660..663
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 673..678
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 685..688
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 690..693
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 695..707
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 728..730
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 732..734
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 745..754
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 759..762
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 766..775
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 780..785
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 791..794
FT /evidence="ECO:0007829|PDB:3H09"
FT TURN 796..798
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 801..804
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 810..813
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 819..823
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 825..827
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 832..842
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 844..846
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 851..854
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 858..861
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 866..882
FT /evidence="ECO:0007829|PDB:3H09"
FT TURN 886..888
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 894..911
FT /evidence="ECO:0007829|PDB:3H09"
FT HELIX 912..914
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 919..926
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 928..938
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 946..950
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 959..965
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 976..980
FT /evidence="ECO:0007829|PDB:3H09"
FT STRAND 983..987
FT /evidence="ECO:0007829|PDB:3H09"
SQ SEQUENCE 1694 AA; 185539 MW; C52427013F93178C CRC64;
MLNKKFKLNF IALTVAYALT PYTEAALVRD DVDYQIFRDF AENKGRFSVG ATNVEVRDKN
NHSLGNVLPN GIPMIDFSVV DVDKRIATLI NPQYVVGVKH VSNGVSELHF GNLNGNMNNG
NAKSHRDVSS 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 KDEIQEAPQM ASETSPKQAK
PAPKEVSTDT KVEETQVQAQ PQTQSTTVAA AEATSPNSKP AEETQPSEKT NAEPVTPVVS
KNQTENTTDQ PTEREKTAKV ETEKTQEPPQ VASQASPKQE QSETVQPQAV LESENVPTVN
NAEEVQAQLQ TQTSATVSTK QPAPENSINT GSATAITETA EKSDKPQTET AASTEDASQH
KANTVADNSV ANNSESSDPK SRRRRSISQP QETSAEETTA ASTDETTIAD NSKRSKPNRR
SRRSVRSEPT VTNGSDRSTV ALRDLTSTNT NAVISDAMAK AQFVALNVGK AVSQHISQLE
MNNEGQYNVW VSNTSMNENY SSSQYRRFSS KSTQTQLGWD QTISNNVQLG GVFTYVRNSN
NFDKASSKNT LAQVNFYSKY YADNHWYLGI DLGYGKFQSN LKTNHNAKFA RHTAQFGLTA
GKAFNLGNFG ITPIVGVRYS YLSNANFALA KDRIKVNPIS VKTAFAQVDL SYTYHLGEFS
VTPILSARYD TNQGSGKINV NQYDFAYNVE NQQQYNAGLK LKYHNVKLSL IGGLTKAKQA
EKQKTAELKL SFSF
