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-MAY-2013, entry version 67.
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 sanguis.
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 / 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 -!- 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 (By similarity).
CC -!- ENZYME REGULATION: Inhibited by EDTA.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall (By similarity).
CC Membrane; Multi-pass membrane protein (By similarity). Secreted,
CC cell wall; Peptidoglycan-anchor (By similarity).
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 -!- SIMILARITY: Belongs to the peptidase M26 family.
CC -!- SIMILARITY: Contains 1 G5 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26901.1; Type=Frameshift; Positions=1833;
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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-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR011098; G5_dom.
DR InterPro; IPR011493; GLUG.
DR InterPro; IPR005877; Gpos_YSIRK.
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 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 Potential.
FT PROPEP 38 99 Potential.
FT /FTId=PRO_0000026839.
FT CHAIN 100 1854 Immunoglobulin A1 protease.
FT /FTId=PRO_0000026840.
FT TRANSMEM 106 125 Helical; (Potential).
FT TRANSMEM 132 154 Helical; (Potential).
FT TOPO_DOM 155 1854 Extracellular (Potential).
FT DOMAIN 256 335 G5.
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 (Potential).
FT ACT_SITE 1495 1495 Probable.
FT METAL 1494 1494 Zinc (Probable).
FT METAL 1498 1498 Zinc (By similarity).
FT METAL 1518 1518 Zinc (By similarity).
FT MOD_RES 99 99 Pentaglycyl murein peptidoglycan amidated
FT threonine (Potential).
FT MUTAGEN 1494 1494 H->F: Loss of activity.
FT MUTAGEN 1495 1495 E->K: Loss of activity.
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
//
