ID O33763_STRSA Unreviewed; 1874 AA.
AC O33763;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 08-NOV-2023, entry version 101.
DE SubName: Full=IgA1 protease {ECO:0000313|EMBL:CAA73856.1};
DE EC=3.4.24.13 {ECO:0000313|EMBL:CAA73856.1};
GN Name=iga {ECO:0000313|EMBL:CAA73856.1};
OS Streptococcus sanguinis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1305 {ECO:0000313|EMBL:CAA73856.1};
RN [1] {ECO:0000313|EMBL:CAA73856.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SK4 {ECO:0000313|EMBL:CAA73856.1};
RX PubMed=9423856;
RA Poulsen K., Reinholdt J., Jespersgaard C., Boye K., Brown T.A., Hauge M.,
RA Kilian M.;
RT "A comprehensive genetic study of streptococcal immunoglobulin A1
RT proteases: evidence for recombination within and between species.";
RL Infect. Immun. 66:181-190(1998).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase M26 family.
CC {ECO:0000256|ARBA:ARBA00005425}.
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DR EMBL; Y13459; CAA73856.1; -; Genomic_DNA.
DR MEROPS; M26.001; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 2.160.20.110; -; 1.
DR Gene3D; 2.20.230.10; Resuscitation-promoting factor rpfb; 1.
DR InterPro; IPR011098; G5_dom.
DR InterPro; IPR011493; GLUG.
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 NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
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 SMART; SM01208; G5; 1.
DR PROSITE; PS51109; G5; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000313|EMBL:CAA73856.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|EMBL:CAA73856.1};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CAA73856.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 107..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..134
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|PROSITE:PS50847"
FT DOMAIN 256..335
FT /note="G5"
FT /evidence="ECO:0000259|PROSITE:PS51109"
FT REGION 566..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1874 AA; 207889 MW; FA30684926BB4532 CRC64;
MKKFFGEKQT RFAFRKLAVG LVSAAISSLF FVSIVGVDSV QAQEKLNVHY KYVTDTEITP
QEKELIVSGF PKMSEGNEET YYLVYRLNSN TGAKTLPNTG DSNNSNTMMT AGLLTTIGLV
VFVVSKRKVQ SKFLLTVLVG AGVGGGLILS VDALENGILL QYNAEYQVSA GESLPSPGEI
SGYTYVGYIK DESIQKLLDN KMLDNQQNAN LDKETLNQNK KLDYSVSFDK NGLKNQTLGV
NTIEPQDEVL FGRVAKPELL YKEENIETEI AFGEQIQENP DLAEGTVRVK QEGKPGRKIE
VARIFTVDNA EVSREVLSTK IEEATPKIVE KGTKKLETPS EKLVASNLVE PEQVAPLPEY
TGVQSGAIVE PEQVASLPEY TGALSGAIVE PEQIEPEIGG VQSGAIVEPE QVTSLPEYTG
VQSGAVVAPE QATPLPEYTE VQAGAVVAPE QVTPLPEYTG TQSGAIVGPE QVTSLPEYTG
TQTGAVVAPE QVTPSPEYTG VQSGAVVAPE QVTPSPEYTG VQSGAVVAPE QVTPLPEYTG
VQSGAIVEPE QVEPPQEYTG NIEPAASEAE NPAEKAQEPK EQKQEPEKNI ELRNVSDVEL
YSLTDGKYKQ HVSLEAIPSN KENYFVKVKS SKFKDVFLPI SSIVDSTKDG QPVYKITASA
EKLKQDIDNK YEDNFTFYLA KKAAKEVTNF TSFSNLVQAI NNDLNGTYYL GASLNANEVE
LENGASSYIK GRFTGKLFGS KDGKNYAIYN LKKPLFDTLS AATVENLALK DANISGKTDI
GALANEANNA TRINNVHVDG VLAGERGIGG LVWKADNSKI KNSSFKGRII NSYETKAPYD
IGGLVGQLTG INAVVDKSKA TITISSNADS TNQTVGGLAG LVEKDALISN SYAEGNINNA
KRFGSVAGVA GYLWDRESNE ERHAGRLHNV LSDVNVMNGN AISGYHYRGM RITDSFSNKD
NRVYKVTLEK DEVVTKESLE ERGTILDASQ IASKKSEINP LSVPIVEPLL TSTNKESDFS
KVEDYQASRA LAYKNIEKLL PFYNKATIVK YGNLVKEDST LFEKEILSAV MMKDNEVITD
IASHKEAANK LLLHYKDHSS EKLDLTYQSD FSKLAEYRVG DTGLIYTPNQ FLHSHSSIIN
EVLPDLRAVD YQSESIRNTL GISSGVSLTE LYLEEQFAKT KENLANTLEK LLSADAVIAS
ENQTINGYVV DKIKRNKEAL LLGLTYLERW YNFNYGDVNI KDLVMYHMDF FGKGNVSPLD
TIIELGKSGF NNLLAKNNVD AYSISLANNN ATKDLFSTLA NYREVFLPNK TNNQWFKEQT
KAYIVEEKSA IDEVKVKQEQ AGSKYSIGVY DRITSDTWKY RNMVLPLLTM PERSVFVIST
ISSLGFGAYD RYRNNEHKAG AELNKFVEDN AQETAKRQRD HYDYWYRILD EQGREKLYRN
ILLYDAYKFG DDATVGKATA EAQFDSSNPA MKYFFGPVGN KVVHNRHGAY ATGDGVYYMG
YRMLDKDGAI TYTHEMTHDS DNEIYLGGYG RRSGLGPEFF AKGLLQAPDH PDDATITVNS
ILKYDKNDVT EKSRLQVLDP TKRFQNADDL KNYVHNMFDV IYMLEYLEGM SIVNRLSDVQ
KVNALRKIDN KYVRDADGND VYATNVIKNI TMADAQKLNS FDSLIENDIL SAREYKNGDV
ERNGYHTIKL FSPIYSALSS EKGTPGDLMG RRMAYELLAA KGFKDGMVPY ISNQYEDDAK
QNGKTISIYG KTRGLVTDDL VLRKVFDGQF NNWTEFKKAM YEERKNKFDS LNKVTFDDTR
QPWTSFATKT ISTVGELQTL MDEAVLKDAN DNWYSWSGYK PEHDSAVHKL KKAVFKAYLD
QTKDFRTSIF ENQK
//
