GenomeNet

Database: UniProt
Entry: Q59986
LinkDB: Q59986
Original site: Q59986 
ID   IGA1_STRSA              Reviewed;        1854 AA.
AC   Q59986;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   29-OCT-2014, entry version 73.
DE   RecName: Full=Immunoglobulin A1 protease;
DE            Short=IgA1 protease;
DE            EC=3.4.24.13;
DE   AltName: Full=IgA-specific zinc metalloproteinase;
DE   Flags: Precursor;
GN   Name=iga;
OS   Streptococcus sanguinis.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 211-219,
RP   FUNCTION, AND MUTAGENESIS OF HIS-1494 AND GLU-1495.
RC   STRAIN=ATCC 10556 / DSM 20567 / JCM 5708 / LMG 14702 / NCIMB 702064 /
RC   NCTC 7863;
RX   PubMed=1987065;
RA   Gilbert J.V., Plaut A.G., Wright A.;
RT   "Analysis of the immunoglobulin A protease gene of Streptococcus
RT   sanguis.";
RL   Infect. Immun. 59:7-17(1991).
CC   -!- FUNCTION: Zinc metalloproteinase which cleaves human
CC       immunoglobulin A1 (IgA1) in the hinge region.
CC       {ECO:0000269|PubMed:1987065}.
CC   -!- CATALYTIC ACTIVITY: Cleavage of Pro-|-Thr bond in the hinge region
CC       of the heavy chain of human IgA.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit. {ECO:0000250}.
CC   -!- ENZYME REGULATION: Inhibited by EDTA.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}. Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Secreted, cell wall {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00477}.
CC   -!- PTM: The Gram-positive cell-wall anchor motif LPXTG is located in
CC       the N-terminal part, in contrast to such motifs in other known
CC       streptococcal and staphylococcal proteins. The protease could be
CC       cleaved by the sortase and anchored in the membrane via the two
CC       potential N-terminal transmembrane domains, whereas the propeptide
CC       located prior to the LPXTG motif would remain attached to the cell
CC       wall peptidoglycan by an amide bond (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M26 family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 G5 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00437}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA26901.1; Type=Frameshift; Positions=1833; Evidence={ECO:0000305};
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L29504; AAA26901.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A60272; A60272.
DR   PIR; B60272; B60272.
DR   ProteinModelPortal; Q59986; -.
DR   MEROPS; M26.001; -.
DR   GO; GO:0005618; C:cell wall; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR011098; G5_dom.
DR   InterPro; IPR011493; GLUG.
DR   InterPro; IPR019948; Gram-positive_anchor.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR011505; Peptidase_M26_C_dom.
DR   InterPro; IPR008006; Peptidase_M26_N_dom.
DR   InterPro; IPR005877; YSIRK_signal_dom.
DR   Pfam; PF07501; G5; 1.
DR   Pfam; PF07581; Glug; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   Pfam; PF07580; Peptidase_M26_C; 1.
DR   Pfam; PF05342; Peptidase_M26_N; 1.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   TIGRFAMs; TIGR01167; LPXTG_anchor; 1.
DR   TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR   PROSITE; PS51109; G5; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Direct protein sequencing; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Peptidoglycan-anchor; Protease;
KW   Repeat; Secreted; Signal; Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL        1     37       {ECO:0000255}.
FT   PROPEP       38     99       {ECO:0000255}.
FT                                /FTId=PRO_0000026839.
FT   CHAIN       100   1854       Immunoglobulin A1 protease.
FT                                /FTId=PRO_0000026840.
FT   TRANSMEM    106    125       Helical. {ECO:0000255}.
FT   TRANSMEM    132    154       Helical. {ECO:0000255}.
FT   TOPO_DOM    155   1854       Extracellular. {ECO:0000255}.
FT   DOMAIN      256    335       G5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00437}.
FT   REPEAT      349    368       1.
FT   REPEAT      369    388       2.
FT   REPEAT      389    406       3.
FT   REPEAT      407    426       4.
FT   REPEAT      427    446       5.
FT   REPEAT      447    466       6.
FT   REPEAT      467    486       7.
FT   REPEAT      487    506       8.
FT   REPEAT      507    526       9.
FT   REPEAT      527    546       10.
FT   REGION      349    546       10 X 20 AA approximate tandem repeats.
FT   MOTIF        96    100       LPXTG sorting signal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00477}.
FT   ACT_SITE   1495   1495       {ECO:0000305}.
FT   METAL      1494   1494       Zinc. {ECO:0000305}.
FT   METAL      1498   1498       Zinc. {ECO:0000250}.
FT   METAL      1518   1518       Zinc. {ECO:0000250}.
FT   MOD_RES      99     99       Pentaglycyl murein peptidoglycan amidated
FT                                threonine. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00477}.
FT   MUTAGEN    1494   1494       H->F: Loss of activity.
FT                                {ECO:0000269|PubMed:1987065}.
FT   MUTAGEN    1495   1495       E->K: Loss of activity.
FT                                {ECO:0000269|PubMed:1987065}.
SQ   SEQUENCE   1854 AA;  206024 MW;  CE2149C0BC7FA4DE CRC64;
     MKKFLGEKQT RFAFRKLAVG LVSAAISSLF FVSIVGVDSV QAQEKLNVHY KYVTDTEITP
     QEKELIVSGV PRMPEGNEET YYLVYRLNSN AGAKTLPNTG DNNSNTMMAA GLLLTTIGLV
     VFAVSKRKVQ SKFLLTVLVG ASVGGGLILS VDALENGSLL QYNAEYQVSA GESLPSPGEI
     SGYTYVGYIK DESIKKLLDN KIPDNQQNAN VDKEALNQNK KLDYSVSFDK NGLKNQTVGV
     NTIEPQDEVL SGRVAKPELL YKETSIETEI AYGEQIQENP DLAEGTVRVK QEGKPGRKIE
     VVRIFTVDNA EVSREVLSTK IEEATPKIVE KGTKKLEAPS EKPVTSNLVQ PEQVAPLPEY
     TGVQSGAIVE PEQVASLPEY SGTLSGAIVE PEQIEPEIGG VQSGAIVEPE QVTPLPEYTG
     TQAGAVVSPE QVAPLPEYTG TQSGAIVEPA QVTPLPEYTG VQSGAIVKPA QVTPLPEYTG
     TQSGAIVEPE QVTPSPEYTG VQAGAIVEPE QVASLPEYTG SQAGAIVEPE QVEPPQEYTG
     NIEPAAPEAE NPTEKAQEPK EQKQEPEKNI ELRNVSDVEL YSLADGKYKQ HVSLDAIPSN
     QENYFVKVKS SKFKDVFLPI SSIVDSTKDG QPVYKITASA EKLKQDVNNK YEDNFTFYLA
     KKAEREVTNF TSFSNLVQAI NNNLNGTYYL AASLNANEVE LENGASSYIK GRFTGKLFGS
     KDGKNYAIYN LKKPLFDTLS AATVENLTLK DVNISGKTDI GALANEANNA TRINNVHVDG
     VLAGERGIGG LVWKADNSKI SNSSFKGRIV NSYETKAPYN IGGLVGQLTG INALVDKSKA
     TITISSNADS TNQTVGGLAG LVEKDALISN SYAEGNINNV KRFGSVAGVA GYLWDRDSSE
     ERHAGRLHNV LSDINVMNGN AISGYHYRGM RITDSYSNKD NRVYKVTLEK DEVVTKESLE
     ERGTILDVSQ IASKKSEINS LSAPKVETLL TSTNKESDFS KVKDYQASRA LAYKNIEKLL
     PFYNKATIVK YGNLVKEDST LYEKEILSAV MMKDNEVITD IASHKEAANK LLIHYKDHSS
     EKLDLTYQSD FSKLAEYRVG DTGLIYTPNQ FLQNHSSIVN EVLPDLKAVD YQSEAIRNTL
     GISSGVSLTE LYLEEQFAKT KENLANTLEK LLSADAVIAS ENQTINGYVV DKIKRNKEAL
     LLGLTYLERW YNFNYGDVNV KDLVMYHMDF FGKGNVSPLD TIIELGKSGF NNLLAKNNVD
     AYNISLANNN ATKDLFSTLA NYREVFLPNK TNNQWFKEQT KAYIVEEKSA IDEVRVKQEQ
     AGSKYSIGVY DRITSDTWKY RNMVLPLLTM PERSVFVIST ISSLGFGAYD RYRNNEHRAG
     AELNKFVEDN AQETAKRQRD HYDYWYRILD EQGREKLYRN ILVYDAYKFG DDTTVDKATV
     EAQFDSSNPA MKYFFGPVGN KVVHNKHGAY ATGDSVYYMG YRMLDKDGAI TYTHEMTHDS
     DNEIYLGGYG RRSGLGPEFF AKGLLQAPDH PDDATITVNS ILKYDKNDAS EKSRLQVLDP
     TKRFQNADDL KNYVHNMFDV IYMLEYLEGM SIVNRLSDVQ KVNALRKIEN KYVRDADGND
     VYATNVIKNI TMADAQKLNS FNSLIENDIL SAREYKNGDV ERNGYHTIKL FSPIYSALSS
     EKGTPGDLMG RRIAYELLAA KGFKDGMVPY ISNQYEDDAK QNGKTISIYG KTRGLVTDDL
     VLRKVFNGQF NNWTEFKKAM YEERKNKFDS LNKVTFDDTR QPWTSYATKT ISTVEELQTL
     MDEAVLQDAN DNWYSWSGYK PEYNSAVHKL KKAVFKAYLD QTKDFRKSIF ENQK
//
DBGET integrated database retrieval system