IgA-specific serine endopeptidase autotransporter precursor

Preferred order of sections

Names and origin

Protein names

Recommended name:
IgA-specific serine endopeptidase autotransporter
EC=3.4.21.72

Cleaved into the following 2 chains:

IgA-specific serine endopeptidase
Alternative name(s):
IgA protease
IgA-specific serine endopeptidase translocator
Alternative name(s):
Helper peptide

Gene names

Name:

iga

Organism

Neisseria gonorrhoeae

Taxonomic identifier

485 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	1532 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This protease is specific for immunoglobulin A.
Catalytic activity	Cleavage of immunoglobulin A molecules at certain Pro-\|-Xaa bonds in the hinge region. No small molecule substrates are known.
Subcellular location	IgA-specific serine endopeptidase autotransporter: Periplasm By similarity. IgA-specific serine endopeptidase: Secreted. Cell surface. IgA-specific serine endopeptidase translocator: Cell outer membrane; Multi-pass membrane protein By similarity. Note: The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane By similarity.
Domain	The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface, with subsequent cleavage.
Sequence similarities	Contains 1 autotransporter (TC 1.B.12) domain. [View classification] Contains 1 peptidase S6 domain.

Ontologies

Keywords
Cellular component	Cell membrane Cell outer membrane Membrane Periplasm Secreted
Domain	Signal Transmembrane Transmembrane beta strand
Molecular function	Hydrolase Protease Serine protease
PTM	Autocatalytic cleavage Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Chain

28 – 1532

1505

IgA-specific serine endopeptidase autotransporter

PRO_0000387603

Chain

28 – 986

959

IgA-specific serine endopeptidase

PRO_0000026968

Chain

987 – 1532

546

IgA-specific serine endopeptidase translocator

PRO_0000026969

Regions

Domain

1280 – 1532

253

Autotransporter

Sites

Active site

278

1

Potential

Site

986 – 987

2

Cleavage; by autolysis

Site

1018 – 1019

2

Cleavage; by autolysis

Site

1121 – 1122

2

Cleavage; by autolysis

Experimental info

Sequence conflict

326

1

H → N Ref.2

Sequence conflict

338

1

H → N Ref.2

Sequence conflict

428

1

N → M Ref.2

Sequence conflict

532

1

H → N Ref.2

Sequence conflict

616

1

I → V Ref.2

Sequence conflict

632

1

H → N Ref.2

Sequence conflict

668

1

K → N Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P09790 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 68FF4112BD22F40D
Show »

FASTA

1,532

168,976

        10         20         30         40         50         60 
MKAKRFKINA ISLSIFLAYA LTPYSEAALV RDDVDYQIFR DFAENKGKFF VGATDLSVKN 

        70         80         90        100        110        120 
KRGQNIGNAL SNVPMIDFSV ADVNKRIATV VDPQYAVSVK HAKAEVHTFY YGQYNGHNDV 

       130        140        150        160        170        180 
ADKENEYRVV EQNNYEPHKA WGASNLGRLE DYNMARFNKF VTEVAPIAPT DAGGGLDTYK 

       190        200        210        220        230        240 
DKNRFSSFVR IGAGRQLVYE KGVYHQEGNE KGYDLRDLSQ AYRYAIAGTP YKDINIDQTM 

       250        260        270        280        290        300 
NTEGLIGFGN HNKQYSAEEL KQALSQDALT NYGVLGDSGS PLFAFDKQKN QWVFLGTYDY 

       310        320        330        340        350        360 
WAGYGKKSWQ EWNIYKKEFA DKIKQHDNAG TVKGNGEHHW KTTGTNSHIG STAVRLANNE 

       370        380        390        400        410        420 
GDANNGQNVT FEDNGTLVLN QNINQGAGGL FFKGDYTVKG ANNDITWLGA GIDVADGKKV 

       430        440        450        460        470        480 
VWQVKNPNGD RLAKIGKGTL EINGTGVNQG QLKVGDGTVI LNQKADADKK VQAFSQVGIV 

       490        500        510        520        530        540 
SGRGTLVLNS SNQINPDNLY FGFRGGRLDA NGNDLTFEHI RNVDEGARIV NHNTDHASTI 

       550        560        570        580        590        600 
TLTGKSLITN PNSLSVHSIQ NDYDEDDYSY YYRPRRPIPQ GKDLYYKNYR YYALKSGGRL 

       610        620        630        640        650        660 
NAPMPENGVA ENNDWIFMGY TQEEARKNAM NHKNNRRIGD FGGFFDEENG KGHNGALNLN 

       670        680        690        700        710        720 
FNGKSAQKRF LLTGGANLNG KISVTQGNVL LSGRPTPHAR DFVNKSSARK DAHFSKNNEV 

       730        740        750        760        770        780 
VFEDDWINRT FKAAEIAVNQ SASFSSGRNV SDITANITAT DNAKVNLGYK NGDEVCVRSD 

       790        800        810        820        830        840 
YTGYVTCNTG NLSDKALNSF DATRINGNVN LNQNAALVLG KAALWGKIQG QGNSRVSLNQ 

       850        860        870        880        890        900 
HSKWHLTGDS QVHNLSLADS HIHLNNASDA QSANKYHTIK INHLSGNGHF HYLTDLAKNL 

       910        920        930        940        950        960 
GDKVLVKESA SGHYQLHVQN KTGEPNQEGL DLFDASSVQD RSRLFVSLAN HYVDLGALRY 

       970        980        990       1000       1010       1020 
TIKTENGITR LYNPYAGNGR PVKPAPSPAA NTASQAQKAT QTDGAQIAKP QNIVVAPPSP 

      1030       1040       1050       1060       1070       1080 
QANQAEEALR QQAKAEQVKR QQAAEAEKVA RQKDEEAKRK AAEIARQQEE ARKAAELAAK 

      1090       1100       1110       1120       1130       1140 
QKAEAERKAR ELARQKAEEA SHQANAKPKR RRRRAILPRP PAPVFSLDDY DAKDNSESSI 

      1150       1160       1170       1180       1190       1200 
GNLARVIPRM GRELINDYEE IPLEELEDEA EEERRQATQF HSKSRNRRAI SSEPSSDEDA 

      1210       1220       1230       1240       1250       1260 
SESVSTSDKH PQDNTELHEK VETAGLQPRA AQPRTQAAAQ ADAVSTNTNS ALSDAMASTQ 

      1270       1280       1290       1300       1310       1320 
SILLDTGAYL TRHIAQKSRA DAEKNSVWMS NTGYGRDYAS AQYRRFSSKR TQTQIGIDRS 

      1330       1340       1350       1360       1370       1380 
LSENMQIGGV LTYSDSQHTF DQAGGKNTFV QANLYGKYYL NDAWYVAGDI GAGSLRSRLQ 

      1390       1400       1410       1420       1430       1440 
TQQKANFNRT SIQTGLTLGN TLKINQFEIV PSAGIRYSRL SSADYKLGDD SVKVSSMAVK 

      1450       1460       1470       1480       1490       1500 
TLTAGLDFAY RFKVGNLTVK PLLSAAYFAN YGKGGVNVGG KSFAYKADNQ QQYSAGVALL 

      1510       1520       1530 
YRNVTLNVNG SITKGKQLEK QKSGQIKIQI RF

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References

[1]	"Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease." Pohlner J., Halter R., Beyreuther K., Meyer T.F. Nature 325:458-462(1987) [PubMed: 3027577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: MS11.
[2]	"Mosaic-like organization of IgA protease genes in Neisseria gonorrhoeae generated by horizontal genetic exchange in vivo." Halter R., Pohlner J., Meyer T.F. EMBO J. 8:2737-2744(1989) [PubMed: 2511009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 281-680 AND 957-1256. Strain: MS11.
[3]	"Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and Hemophilus influenzae by peptide prolyl boronic acids." Bachovchin W.W., Plaut A.G., Flentke G.R., Lynch M., Kettner C.A. J. Biol. Chem. 265:3738-3743(1990) [PubMed: 2105953] [Abstract] Cited for: ACTIVE SITE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X04835 Genomic DNA. Translation: CAA28538.1.
PIR	A26039.
3D structure databases
ProteinModelPortal	P09790.
ModBase	Search...
Protein family/group databases
MEROPS	S06.001.
TCDB	1.B.12.3.1. autotransporter-1 (AT-1) family.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR005546. Auto_transptbeta. IPR012332. P22_tailspike_C-like. IPR011050. Pectin_lyase_fold/virulence. IPR000710. Peptidase_S6. IPR004899. Pertactin_central. [Graphical view]
Gene3D	G3DSA:2.160.20.20. P22_tailspike. 1 hit.
Pfam	PF03797. Autotransporter. 1 hit. PF02395. Peptidase_S6. 1 hit. PF03212. Pertactin. 1 hit. [Graphical view]
PRINTS	PR00921. IGASERPTASE.
SMART	SM00869. Autotransporter. 1 hit. [Graphical view]
SUPFAM	SSF103515. Auto_transptbeta. 1 hit. SSF51126. Pectin_lyas_like. 1 hit.
PROSITE	PS51208. AUTOTRANSPORTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
PMAP-CutDB	P09790.

Entry information

Entry name

IGA_NEIGO

Accession

Primary (citable) accession number: P09790

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	December 14, 2011
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Family and domain databases

Other

Entry information

Relevant documents