ID A0A1L3MNH2_9BACI Unreviewed; 273 AA.
AC A0A1L3MNH2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase {ECO:0000256|HAMAP-Rule:MF_00727};
DE EC=2.3.2.13 {ECO:0000256|HAMAP-Rule:MF_00727};
DE AltName: Full=Transglutaminase {ECO:0000256|HAMAP-Rule:MF_00727};
DE Short=TGase {ECO:0000256|HAMAP-Rule:MF_00727};
GN Name=tgl {ECO:0000256|HAMAP-Rule:MF_00727};
GN ORFNames=A9C19_03485 {ECO:0000313|EMBL:APH03898.1};
OS Bacillus weihaiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1547283 {ECO:0000313|EMBL:APH03898.1, ECO:0000313|Proteomes:UP000181936};
RN [1] {ECO:0000313|EMBL:APH03898.1, ECO:0000313|Proteomes:UP000181936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alg07 {ECO:0000313|EMBL:APH03898.1,
RC ECO:0000313|Proteomes:UP000181936};
RX PubMed=27901120; DOI=10.1038/srep38248;
RA Zhu Y., Chen P., Bao Y., Men Y., Zeng Y., Yang J., Sun J., Sun Y.;
RT "Complete genome sequence and transcriptomic analysis of a novel marine
RT strain Bacillus weihaiensis reveals the mechanism of brown algae
RT degradation.";
RL Sci. Rep. 6:38248-38248(2016).
CC -!- FUNCTION: Probably plays a role in the assembly of the spore coat
CC proteins by catalyzing epsilon-(gamma-glutamyl)lysine cross-links.
CC {ECO:0000256|HAMAP-Rule:MF_00727}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00727};
CC -!- SIMILARITY: Belongs to the bacillus TGase family. {ECO:0000256|HAMAP-
CC Rule:MF_00727}.
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DR EMBL; CP016020; APH03898.1; -; Genomic_DNA.
DR RefSeq; WP_072578692.1; NZ_CP016020.1.
DR AlphaFoldDB; A0A1L3MNH2; -.
DR STRING; 1547283.A9C19_03485; -.
DR KEGG; bwh:A9C19_03485; -.
DR OrthoDB; 1845399at2; -.
DR Proteomes; UP000181936; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00727; Tgl; 1.
DR InterPro; IPR020916; Gln_gamma-glutamylTfrase_bac.
DR Pfam; PF20085; TGL; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_00727};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000181936};
KW Sporulation {ECO:0000256|HAMAP-Rule:MF_00727};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00727, ECO:0000313|EMBL:APH03898.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 111..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 273 AA; 31402 MW; 8E19FF77FEF13FED CRC64;
MITIGNKVAS GNQLSSQSLS PEQIEMVEKM NRYPNNYVFS SYSHFQFTLM LRQHIIQASR
NLLASKVKFR TFRTSYCNGQ YWQLTNQGGF KLKPQARPSE AIQDIYENGR LYGFECATAI
VIIFYTAVLY SIDHQQFDRL YQGLYLRDWQ SDEDLPIYTR RGNDFLPGDC LYFKNPQFDP
NTPQWQGENV IDLGNDLYFG HGIGIKTAEG IVESLNKKRS PYATESAHLL SQVTRIDDSY
LFQFASGLSR GLHVNFITSK KIAARVGRNY FSL
//
