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Database: UniProt
Entry: I4C9W8_DESTA
LinkDB: I4C9W8_DESTA
Original site: I4C9W8_DESTA 
ID   I4C9W8_DESTA            Unreviewed;       613 AA.
AC   I4C9W8;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Peptidoglycan glycosyltransferase {ECO:0000313|EMBL:AFM26359.1};
DE            EC=2.4.1.129 {ECO:0000313|EMBL:AFM26359.1};
GN   OrderedLocusNames=Desti_3714 {ECO:0000313|EMBL:AFM26359.1};
OS   Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC   Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC   Desulfomonilaceae; Desulfomonile.
OX   NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM26359.1, ECO:0000313|Proteomes:UP000006055};
RN   [1] {ECO:0000313|Proteomes:UP000006055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC   {ECO:0000313|Proteomes:UP000006055};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA   Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR   EMBL; CP003360; AFM26359.1; -; Genomic_DNA.
DR   RefSeq; WP_014811487.1; NC_018025.1.
DR   AlphaFoldDB; I4C9W8; -.
DR   STRING; 706587.Desti_3714; -.
DR   KEGG; dti:Desti_3714; -.
DR   PATRIC; fig|706587.4.peg.4223; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_1_2_7; -.
DR   OrthoDB; 9766847at2; -.
DR   Proteomes; UP000006055; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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   InterPro; IPR017790; Penicillin-binding_protein_2.
DR   NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 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:AFM26359.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006055};
KW   Transferase {ECO:0000313|EMBL:AFM26359.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          62..231
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          264..599
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   613 AA;  67649 MW;  1DB982B494AEED1B CRC64;
     MAELPTQEHF RDRIDLRVRI AIILMTLLMG VLAAKLWHLQ LIQGDAYNEK SDSNRVRLAR
     LTPTRGRILD VKGRVLAENT PSFVLSIVPG ELEKPVELIQ SYAPILGITP ERMRNSIERS
     RNLPKYMHYP VKKNMSLEEV SLVRSRMSES RGVLLEVKPL RLYPGQDNLC HVIGTTGEIS
     QDELAKASRV GYQTGDSLGK TGIEKEYEAY LRGEEGWEQV EIDAKGRTLA TMARKPPKNG
     ADVILTVDSA FQRFVEEVFI HRAGSVVALD PDTGRVLAMV SKPGFDLNLF SPSISERQWK
     TLNSDPLHPL ENRATRGLYS PASTFKAITA LAALSEKVVT PDKKFVCKGQ LELGGQVFRC
     WNPYGHGRVD LHRGIVESCD TYFYELGLKL GPDRIAKYAS LFGMGAPTGV GLPQELPGLV
     PTSAWKMRAY GDSWKDGETL TVAIGQGYLV CTPIQLAVMT AALSNGGKVF KPSIVSQIVA
     ADGTTVFNHS PVVRWEIPID PYHLSLLDSA LVDVVTDKKG TGKRCRIPGI KVHAKTGTSQ
     VIRVKQRTKE EDQIPYHERT HAMFIAYVND RPQKIALIII VEHGGGGGAS AAPLARKILA
     RYYGVPDPGD PED
//
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