ID   TGAS_STRCJ              Reviewed;         416 AA.
AC   Q8GR90;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Protein-glutamine gamma-glutamyltransferase;
DE            EC=2.3.2.13;
DE   AltName: Full=Transglutaminase;
DE            Short=TGase;
DE   Flags: Precursor;
OS   Streptomyces cinnamoneus (Streptoverticillium cinnamoneum).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces cinnamoneus group.
OX   NCBI_TaxID=53446;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11874 / DSM 40005 / NBRC 12852 / JCM 4633 / NCIMB 8851 / NRRL
RC   B-1285 / VKM Ac-876;
RA   Yokoyama K.;
RT   "Streptoverticillium cinnamoneum IFO12852 TGase gene.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the cross-linking of proteins and the conjugation
CC       of polyamines to proteins. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-
CC         lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816,
CC         Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011,
CC         ChEBI:CHEBI:138370; EC=2.3.2.13;
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the bacterial TGase family. {ECO:0000305}.
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DR   EMBL; AB085698; BAC24766.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8GR90; -.
DR   SMR; Q8GR90; -.
DR   BRENDA; 2.3.2.13; 5995.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.1360.10; -; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR015107; Transglut_prok.
DR   InterPro; IPR037084; Transglut_prok_sf.
DR   Pfam; PF09017; Transglut_prok; 1.
DR   PIRSF; PIRSF037210; Transglut_prok; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Signal; Transferase; Zymogen.
FT   SIGNAL          1..29
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   PROPEP          30..85
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000033658"
FT   CHAIN           86..416
FT                   /note="Protein-glutamine gamma-glutamyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT                   /id="PRO_0000033659"
FT   REGION          64..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        340
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        359
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   416 AA;  46394 MW;  677DA9778829839D CRC64;
     MHKRRRLLAF ATVGAVICTA GFTPSVSQAA SSGDGEEKGS YAETHGLTAD DVESINALNE
     RALTLGQPGK PPKELPPSAS APSRAPSDDR ETPPAEPLDR MPEAYRAYGG RATTVVNNYI
     RKWQQVYSHR DGKKQQMTEE QREKLSYGCV GVTWVNSGPY PTNRLAFASF DENKYKNDLK
     NTSPRPDETR AEFEGRIAKG SFDEGKGFKR ARDVASVMNK ALENAHDEGT YINNLKTELT
     NNNDALLRED SRSNFYSALR NTPSFKERDG GNYDPSKMKA VIYSKHFWSG QDQRGSSDKR
     KYGDPEAFRP DQGTGLVDMS KDRSIPRSPA KPGEGWVNFD YGWFGAQTEA DADKTTWTHG
     DHYHAPNSDL GPMHVHESKF RKWSAGYADF DRGAYVITFI PKSWNTAPAK VEQGWP