ID A0A1X7AKN5_9GAMM Unreviewed; 691 AA.
AC A0A1X7AKN5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Protein-glutamine gamma-glutamyltransferase {ECO:0000313|EMBL:SMA47559.1};
DE EC=2.3.2.13 {ECO:0000313|EMBL:SMA47559.1};
GN Name=tgpA {ECO:0000313|EMBL:SMA47559.1};
GN ORFNames=EHSB41UT_02463 {ECO:0000313|EMBL:SMA47559.1};
OS Parendozoicomonas haliclonae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Parendozoicomonas.
OX NCBI_TaxID=1960125 {ECO:0000313|EMBL:SMA47559.1, ECO:0000313|Proteomes:UP000196573};
RN [1] {ECO:0000313|EMBL:SMA47559.1, ECO:0000313|Proteomes:UP000196573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB41UT1 {ECO:0000313|EMBL:SMA47559.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FWPT01000005; SMA47559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7AKN5; -.
DR OrthoDB; 9804872at2; -.
DR Proteomes; UP000196573; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.10.620.30; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025403; TgpA-like_C.
DR InterPro; IPR021878; TgpA_N.
DR InterPro; IPR002931; Transglutaminase-like.
DR PANTHER; PTHR42736; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR PANTHER; PTHR42736:SF1; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
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; Cysteine proteinases; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:SMA47559.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000196573};
KW Transferase {ECO:0000313|EMBL:SMA47559.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 435..505
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
SQ SEQUENCE 691 AA; 77736 MW; 4C391B9E40E56108 CRC64;
MLNSLLNKEW LRRKRKTAPA VAPVTRAASF SLVFILVLVC LPLAPLLPAG TWVLVSLVVG
WRLILLRARG AHPGKLIRTL LVVVALALVL LHYGTLLGLE AGATTLVSAY TLKLLEMRSR
RDALVLSFMG FFVVVTGLLF SQSIAMTGYL LVCLVALVSV LVGLHQPGTQ TDIGPALRTG
LLLSAQALPL MVILFVLVPR IPPLWAVPHP DNSARTGLSD EMAPGDIARL SQSGELAFRA
TFTGEVPPPE QRYWRAVVMY WFDGRRWSQG DQKDWQKVGV AEEELISWYP QKPAWAPEQS
SANVDYRYDI ILEPSGRPWL PVLGPVNTAV QGTGLTRDWR LLSRDNVDLL RQYSMPSSGF
QGMDAELPTW LKAASLQLPA TGNARARQWA EELASQYGSN TPALVSVVLR HFREQDYYYT
LRPPTLSGNT IDAFLFDTRR GFCAHYAGAL TFILRAAGIP SRVVAGYQGG EVKEGGVVQV
RQFDAHAWVE YWQAGYGWQR VDPTAAVAPE RVEQGLEQAV AEEGSFLEGN LFSPVRYRHI
DWVNTLRLQY EQLEYQWQRL VLSYDEDAQK DLFKDLFPGK DTLTVLLQLL VITVLLVMVI
SLIWVTRPWQ QKLAPADRYY QQFCQRMKRK GLPRHPGEGP EDYALRIKRE RPEWGQKAQE
VTELYIRLAY ANQEPQSHEA TLQQLKRLAC I
//
