TGPA_PSEAE
ID TGPA_PSEAE Reviewed; 668 AA.
AC Q9HZX3;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein-glutamine gamma-glutamyltransferase;
DE EC=2.3.2.13;
DE AltName: Full=Transglutaminase protein A;
DE Short=TGase A;
GN Name=tgpA; OrderedLocusNames=PA2873;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, GENE NAME, DOMAIN, SUBCELLULAR LOCATION,
RP TOPOLOGY, DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=23209712; DOI=10.1371/journal.pone.0050323;
RA Milani A., Vecchietti D., Rusmini R., Bertoni G.;
RT "TgpA, a protein with a eukaryotic-like transglutaminase domain, plays a
RT critical role in the viability of Pseudomonas aeruginosa.";
RL PLoS ONE 7:E50323-E50323(2012).
CC -!- FUNCTION: Displays transglutaminase activity (TGase) in vitro. Plays a
CC critical role in the viability of P.aeruginosa. Might contribute to an
CC essential function linked to the cell wall.
CC {ECO:0000269|PubMed:23209712}.
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 Evidence={ECO:0000269|PubMed:23209712};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:23209712}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23209712}.
CC -!- INDUCTION: Is expressed in both exponential and stationary phases of
CC growth. Appears to be part of an operon together with PA2874 and
CC PA2875. {ECO:0000269|PubMed:23209712}.
CC -!- DOMAIN: The transglutaminase activity is contained within the
CC periplasmic domain (180-544). {ECO:0000269|PubMed:23209712}.
CC -!- DISRUPTION PHENOTYPE: Disruption experiments show that tgpA is
CC essential. {ECO:0000269|PubMed:23209712}.
CC -!- MISCELLANEOUS: Unlike Guinea pig TGase, TGase activity is not affected
CC by EDTA addition, suggesting that TGase activity is Ca(2+)-independent,
CC similar to members of the bacterial transglutaminase family.
CC {ECO:0000305|PubMed:23209712}.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG06261.1; -; Genomic_DNA.
DR PIR; F83287; F83287.
DR RefSeq; NP_251563.1; NC_002516.2.
DR RefSeq; WP_003114743.1; NZ_QZGE01000011.1.
DR PDB; 6G49; X-ray; 1.60 A; A=180-499.
DR PDB; 6G4H; X-ray; 1.80 A; A=180-499.
DR PDBsum; 6G49; -.
DR PDBsum; 6G4H; -.
DR AlphaFoldDB; Q9HZX3; -.
DR SMR; Q9HZX3; -.
DR STRING; 287.DR97_5068; -.
DR PaxDb; Q9HZX3; -.
DR PRIDE; Q9HZX3; -.
DR EnsemblBacteria; AAG06261; AAG06261; PA2873.
DR GeneID; 882644; -.
DR KEGG; pae:PA2873; -.
DR PATRIC; fig|208964.12.peg.3014; -.
DR PseudoCAP; PA2873; -.
DR HOGENOM; CLU_012397_0_0_6; -.
DR InParanoid; Q9HZX3; -.
DR OMA; QFDAHAW; -.
DR PhylomeDB; Q9HZX3; -.
DR BioCyc; PAER208964:G1FZ6-2923-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IDA:UniProtKB.
DR InterPro; IPR025403; DUF4129.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR021878; TgpA_N.
DR InterPro; IPR002931; Transglutaminase-like.
DR Pfam; PF13559; DUF4129; 1.
DR Pfam; PF11992; TgpA_N; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cell inner membrane; Cell membrane;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..668
FT /note="Protein-glutamine gamma-glutamyltransferase"
FT /id="PRO_0000422419"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..50
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..103
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..548
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..668
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 404
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 448
FT /evidence="ECO:0000250"
FT ACT_SITE 464
FT /evidence="ECO:0000250"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6G49"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:6G49"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:6G49"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:6G49"
FT HELIX 331..336
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:6G49"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:6G49"
FT HELIX 362..375
FT /evidence="ECO:0007829|PDB:6G49"
FT HELIX 391..397
FT /evidence="ECO:0007829|PDB:6G49"
FT HELIX 404..417
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:6G49"
FT TURN 435..438
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:6G49"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 447..455
FT /evidence="ECO:0007829|PDB:6G49"
FT TURN 456..458
FT /evidence="ECO:0007829|PDB:6G49"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:6G49"
FT HELIX 465..468
FT /evidence="ECO:0007829|PDB:6G49"
FT HELIX 471..476
FT /evidence="ECO:0007829|PDB:6G49"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:6G49"
SQ SEQUENCE 668 AA; 74807 MW; 646CD6D34F6E96D4 CRC64;
MNAIPRVALV WLLVAQVLVI LPHLAYMPLW IAAMWLGCAA WRVQVFRMRA GYPRAWVKLA
LALLAGAGVW LSRGSLVGLD AGAVLLIAAF ILKLVEMKTR RDALVLVFLG FFAVVVGYLF
DDGFLAALYS LLPVTALLAA LIGLQQSAFA SRPWPTLRLA GGLLLQALPL MLLLFLFFPR
LGPLWSLPMP GNKGVTGLSE SMAPGDIAEL GRSAELAFRV RFEGALPPRE QLYWRALTME
RFDGRRWAQA PQWSGEDALH WQKRGPELRY DVIMQPSSQP WLFALDVAQT DQTDTRLMSD
FHLQRRQPVE QRLFYRVSSW PQALRESSID PRTRWRNLQL PMHGNPRARA LADELRQAHA
QPQALVAALL QRFNHEPFAY TLKPPATGAD GVDDFLFDTR SGFCAHYAGA MAFVLRAAGI
PARVVAGYQG GELNPAGNYL LVHQFDAHAW VEYWQPEQGW LSVDPTYQVA PERIEQGLEQ
ALAGDSEYLA DAPLSPLRYR GLPWLNDMRL AWDSLNYGWQ RWVLAYQGEQ QGAFLQRWFG
GLDPTRLGLL LGAAAILSVG LLALFLLKPW QGRGDLRSRQ LRRFERLLEM HGLRRSPGEG
LRSYGERAAR VLPAQAPAIA AFVGAFEAQR YGHGGADDPG LRLRALRRAL PWRLVRTPTR
DGRGEEQA
