ID A5JSJ3_STRSU Unreviewed; 1121 AA.
AC A5JSJ3;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Transglutaminase-like domain-containing protein {ECO:0000259|Pfam:PF01841};
OS Streptococcus suis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1307 {ECO:0000313|EMBL:ABQ42881.1};
RN [1] {ECO:0000313|EMBL:ABQ42881.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=260 {ECO:0000313|EMBL:ABQ42881.1};
RA Gu H., Lu C.;
RT "Newly identified complete ivi genes of Streptococcus suis serotype 2.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007829|PDB:4XZ7}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 39-437.
RX PubMed=26085092; DOI=10.1074/jbc.m115.643338;
RA Yu J., Pian Y., Ge J., Guo J., Zheng Y., Jiang H., Hao H., Yuan Y.,
RA Jiang Y., Yang M.;
RT "Functional and Structural Characterization of the Antiphagocytic
RT Properties of a Novel Transglutaminase from Streptococcus suis.";
RL J. Biol. Chem. 290:19081-19092(2015).
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DR EMBL; EF563979; ABQ42881.1; -; Genomic_DNA.
DR RefSeq; WP_012027720.1; NZ_WODB01000005.1.
DR PDB; 4XZ7; X-ray; 2.10 A; A/B=39-437.
DR PDBsum; 4XZ7; -.
DR AlphaFoldDB; A5JSJ3; -.
DR SMR; A5JSJ3; -.
DR GeneID; 8153628; -.
DR PATRIC; fig|1307.469.peg.571; -.
DR OMA; RITRAWD; -.
DR BRENDA; 2.3.2.13; 7186.
DR Gene3D; 3.10.620.30; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR Pfam; PF01841; Transglut_core; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4XZ7}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..1121
FT /note="Transglutaminase-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039309613"
FT DOMAIN 247..348
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|Pfam:PF01841"
FT REGION 553..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1121 AA; 122046 MW; 35E190AC94FC5179 CRC64;
MIPIQQHGKR WLILTLTLST SVLALASIGT SQPVVFADEN SHLQSPKNTN KIEVLNWEAF
SKKLKDYSSD QRQFHVLKLG FENRLGTLST REELEEFGKN NNFLVINGKV TQNIHDFPHI
LVMNKGDVIA HNEEDYHNQM RELRFSGNGD LHNSMEPKRI HALFKIELDS NKRQLLNAAG
LGTAENSLKN INGMTIYSHG LTVDNKYYED YSKYTHNSVK NINVTKERFI ANDDLIHKLI
ESSEAMKQSS ERDKVKAFVQ YVANHTTYDW EAANKAVQNY ADINYYLGSD LFAVTERQKA
MCVGFSTTAA RAFNMLGLPA YVVVGKNAEG VPHATARVYY DKKWHTIDGT GFITGNKHQR
SAKYSEKHFS TIGEDSYDVV EAGQEPKAER NYMIIDSNYE SWAMKQKTAD LLLFNKEKSL
VGLDYIAYVE PTYITENKKN HLLDIYKALK RKVEETKATD KDDKDDKQEG YDRVLQFVNS
DIDKLSALSK ITEEEFKALE NSMDLARVFL GQMNAKAGKE FSEGETYQSY LKNRQKNNTN
SDDDRNRNEL QENQANSDEV SQNSKDASAP SVNSAQQSEE LEGTPSTQET ISAAPSQQTP
AAPKALQAKT ELEDKTETSS LGNTEMVSPS SETAQNTVDS KEESDAKLPY VEPSSKESSE
AQVNTVSSPQ VSSASPTSSE TISTDTVTAS QEKAESRVSA PQVISASQTS PETNSAEVVT
TSQEVAKAPV SAPQVSSEIQ TLSETAPTEV ATEAPELSAL ESNPAPQTSL ETTPTEEVTE
TPEPSVVESN SASPTSPETN SAEAVTTSQE MAEPSVSVPQ VSSEIPTSSE TAPAEVATEV
SEESSSASQP SPETTPTETV TTSQEVAEAP VSAPQVSSEI PTSPETASTE VVVAKQEVAD
SPVSAPQVIS EIPTSSETAP AEVATEVTEP SVVASSSASP TSPEANSTEV VVAKQEVADP
LVSAPQTSSA SLTLEVPKNE HLDEKADATT PNGVEANTHE AVSVPTSDIR VQDAGSDTVP
QPYSLSATLF EEAISTVEPV GVATSSQERS AVAGKVKVPT SLERSNNSVE EEKVVDSNAT
IENREPEKKE ILTSENVLNS LVTIWVALST SFFMRYFSRG K
//
