ID E8T2P5_THEA1 Unreviewed; 674 AA.
AC E8T2P5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:ADU97140.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:ADU97140.1};
GN OrderedLocusNames=Theam_1176 {ECO:0000313|EMBL:ADU97140.1};
OS Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1).
OC Bacteria; Aquificota; Aquificae; Desulfurobacteriales;
OC Desulfurobacteriaceae; Thermovibrio.
OX NCBI_TaxID=648996 {ECO:0000313|EMBL:ADU97140.1, ECO:0000313|Proteomes:UP000006362};
RN [1] {ECO:0000313|EMBL:ADU97140.1, ECO:0000313|Proteomes:UP000006362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15698 / JCM 12110 / HB-1
RC {ECO:0000313|Proteomes:UP000006362};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Vetriani C., Woyke T.;
RT "Complete sequence of chromosome of Thermovibrio ammonificans HB-1.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002444; ADU97140.1; -; Genomic_DNA.
DR RefSeq; WP_013537926.1; NC_014926.1.
DR AlphaFoldDB; E8T2P5; -.
DR STRING; 648996.Theam_1176; -.
DR KEGG; tam:Theam_1176; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_0_0; -.
DR OrthoDB; 9770103at2; -.
DR Proteomes; UP000006362; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.450.330; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:ADU97140.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:ADU97140.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..280
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 317..630
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 674 AA; 77332 MW; 01D5F065A58E5556 CRC64;
MRPIYWLREL ILRVYRFIKP FKEDRLNLFF LFSLALLTVY SVRLLYLTHF DREEWIKFVN
RQFSGKIKIS YERGEILDRN GSLLAASERV VSFYVRPTEI KDWKLFCQIV TLQKAPLEEY
AEEKGVSLEK LYELLKPLKE VTPEELQKAY EKKYTVVTYK GKKIKVPFVW LHKKAQTTPY
RAAKAVKVAM RIYYTLSGES PIKKRHPDIL GFVPEYKRCY PYGVGSTVVG LASDFDKGLS
NLEYYLDKKG IITGKTVLLS GEKDYLGRVY LGKNASQFLT KEKGNNVLLT IDGNLQYIVE
KTISEYGKKW HPKFINAVLM DPNTGEILAA ASWPFYRYGE KLKKGDTSKL VARYVTDVYE
PGSVMKPIVL AAALNEGVVG VNDVFYCPAR IKINDRTFTN EFHGRNVKLR AWEIIEYSDN
VGIIQVAQKL GKKKLYEYLK RFGFGNKTGI ELPIESKGLL SNWKKWKDVE FATITFGYHI
SVTTLQLAAA YSALVNGGIY YKPFLIKAIL DEKGNVIKSF SPVAERRVIS ERTSKLMRRV
LTMVVEGGTA KPTKFENFYV GGKTGTAQKL IKEKGKKPHY SRKKIYATFV GFFPATNPKY
VLAVTVNEPK VPKNMLWATK IAVPIFRDIA ERVLLYERTA PDKKRYTVEP GGNITATEIN
TDFPFKNGIQ QRKK
//
