IGA_NEIGO
ID IGA_NEIGO Reviewed; 1532 AA.
AC P09790;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=IgA-specific serine endopeptidase autotransporter;
DE EC=3.4.21.72;
DE Contains:
DE RecName: Full=IgA-specific serine endopeptidase;
DE AltName: Full=IgA protease;
DE Contains:
DE RecName: Full=IgA-specific serine endopeptidase translocator;
DE AltName: Full=Helper peptide;
DE Flags: Precursor;
GN Name=iga;
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=MS11;
RX PubMed=3027577; DOI=10.1038/325458a0;
RA Pohlner J., Halter R., Beyreuther K., Meyer T.F.;
RT "Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA
RT protease.";
RL Nature 325:458-462(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-680 AND 957-1256.
RC STRAIN=MS11;
RX PubMed=2511009; DOI=10.1002/j.1460-2075.1989.tb08415.x;
RA Halter R., Pohlner J., Meyer T.F.;
RT "Mosaic-like organization of IgA protease genes in Neisseria gonorrhoeae
RT generated by horizontal genetic exchange in vivo.";
RL EMBO J. 8:2737-2744(1989).
RN [3]
RP ACTIVE SITE.
RX PubMed=2105953; DOI=10.1016/s0021-9258(19)39656-5;
RA Bachovchin W.W., Plaut A.G., Flentke G.R., Lynch M., Kettner C.A.;
RT "Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and Hemophilus
RT influenzae by peptide prolyl boronic acids.";
RL J. Biol. Chem. 265:3738-3743(1990).
CC -!- FUNCTION: This protease is specific for immunoglobulin A.
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: [IgA-specific serine endopeptidase
CC autotransporter]: Periplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [IgA-specific serine endopeptidase]: Secreted.
CC Cell surface.
CC -!- SUBCELLULAR LOCATION: [IgA-specific serine endopeptidase translocator]:
CC Cell 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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X04835; CAA28538.1; -; Genomic_DNA.
DR PIR; A26039; A26039.
DR AlphaFoldDB; P09790; -.
DR SMR; P09790; -.
DR BindingDB; P09790; -.
DR ChEMBL; CHEMBL3970; -.
DR MEROPS; S06.001; -.
DR TCDB; 1.B.12.3.1; the autotransporter-1 (at-1) family.
DR PRIDE; P09790; -.
DR KEGG; ag:CAA28538; -.
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 Autocatalytic cleavage; Cell outer membrane; Direct protein sequencing;
KW Hydrolase; Membrane; Periplasm; Protease; Secreted; Serine protease;
KW Signal; Transmembrane; Transmembrane beta strand; Zymogen.
FT SIGNAL 1..27
FT CHAIN 28..1532
FT /note="IgA-specific serine endopeptidase autotransporter"
FT /id="PRO_0000387603"
FT CHAIN 28..986
FT /note="IgA-specific serine endopeptidase"
FT /id="PRO_0000026968"
FT CHAIN 987..1532
FT /note="IgA-specific serine endopeptidase translocator"
FT /id="PRO_0000026969"
FT DOMAIN 28..322
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1280..1532
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 979..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 278
FT /evidence="ECO:0000255"
FT SITE 986..987
FT /note="Cleavage; by autolysis"
FT SITE 1018..1019
FT /note="Cleavage; by autolysis"
FT SITE 1121..1122
FT /note="Cleavage; by autolysis"
FT CONFLICT 326
FT /note="H -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="H -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="N -> M (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="H -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 616
FT /note="I -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="H -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 668
FT /note="K -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1532 AA; 168976 MW; 68FF4112BD22F40D CRC64;
MKAKRFKINA ISLSIFLAYA LTPYSEAALV RDDVDYQIFR DFAENKGKFF VGATDLSVKN
KRGQNIGNAL SNVPMIDFSV ADVNKRIATV VDPQYAVSVK HAKAEVHTFY YGQYNGHNDV
ADKENEYRVV EQNNYEPHKA WGASNLGRLE DYNMARFNKF VTEVAPIAPT DAGGGLDTYK
DKNRFSSFVR IGAGRQLVYE KGVYHQEGNE KGYDLRDLSQ AYRYAIAGTP YKDINIDQTM
NTEGLIGFGN HNKQYSAEEL KQALSQDALT NYGVLGDSGS PLFAFDKQKN QWVFLGTYDY
WAGYGKKSWQ EWNIYKKEFA DKIKQHDNAG TVKGNGEHHW KTTGTNSHIG STAVRLANNE
GDANNGQNVT FEDNGTLVLN QNINQGAGGL FFKGDYTVKG ANNDITWLGA GIDVADGKKV
VWQVKNPNGD RLAKIGKGTL EINGTGVNQG QLKVGDGTVI LNQKADADKK VQAFSQVGIV
SGRGTLVLNS SNQINPDNLY FGFRGGRLDA NGNDLTFEHI RNVDEGARIV NHNTDHASTI
TLTGKSLITN PNSLSVHSIQ NDYDEDDYSY YYRPRRPIPQ GKDLYYKNYR YYALKSGGRL
NAPMPENGVA ENNDWIFMGY TQEEARKNAM NHKNNRRIGD FGGFFDEENG KGHNGALNLN
FNGKSAQKRF LLTGGANLNG KISVTQGNVL LSGRPTPHAR DFVNKSSARK DAHFSKNNEV
VFEDDWINRT FKAAEIAVNQ SASFSSGRNV SDITANITAT DNAKVNLGYK NGDEVCVRSD
YTGYVTCNTG NLSDKALNSF DATRINGNVN LNQNAALVLG KAALWGKIQG QGNSRVSLNQ
HSKWHLTGDS QVHNLSLADS HIHLNNASDA QSANKYHTIK INHLSGNGHF HYLTDLAKNL
GDKVLVKESA SGHYQLHVQN KTGEPNQEGL DLFDASSVQD RSRLFVSLAN HYVDLGALRY
TIKTENGITR LYNPYAGNGR PVKPAPSPAA NTASQAQKAT QTDGAQIAKP QNIVVAPPSP
QANQAEEALR QQAKAEQVKR QQAAEAEKVA RQKDEEAKRK AAEIARQQEE ARKAAELAAK
QKAEAERKAR ELARQKAEEA SHQANAKPKR RRRRAILPRP PAPVFSLDDY DAKDNSESSI
GNLARVIPRM GRELINDYEE IPLEELEDEA EEERRQATQF HSKSRNRRAI SSEPSSDEDA
SESVSTSDKH PQDNTELHEK VETAGLQPRA AQPRTQAAAQ ADAVSTNTNS ALSDAMASTQ
SILLDTGAYL TRHIAQKSRA DAEKNSVWMS NTGYGRDYAS AQYRRFSSKR TQTQIGIDRS
LSENMQIGGV LTYSDSQHTF DQAGGKNTFV QANLYGKYYL NDAWYVAGDI GAGSLRSRLQ
TQQKANFNRT SIQTGLTLGN TLKINQFEIV PSAGIRYSRL SSADYKLGDD SVKVSSMAVK
TLTAGLDFAY RFKVGNLTVK PLLSAAYFAN YGKGGVNVGG KSFAYKADNQ QQYSAGVALL
YRNVTLNVNG SITKGKQLEK QKSGQIKIQI RF
