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Database: UniProt
Entry: A0A077FIC1_9PSED
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ID   A0A077FIC1_9PSED        Unreviewed;       777 AA.
AC   A0A077FIC1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=PSAKL28_47040 {ECO:0000313|EMBL:AIL63844.1};
OS   Pseudomonas alkylphenolica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=237609 {ECO:0000313|EMBL:AIL63844.1, ECO:0000313|Proteomes:UP000028931};
RN   [1] {ECO:0000313|EMBL:AIL63844.1, ECO:0000313|Proteomes:UP000028931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KL28 {ECO:0000313|EMBL:AIL63844.1,
RC   ECO:0000313|Proteomes:UP000028931};
RA   Lee K., Lim J.Y., Hwang I.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000256|ARBA:ARBA00023988};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR   EMBL; CP009048; AIL63844.1; -; Genomic_DNA.
DR   RefSeq; WP_038615040.1; NZ_CP009048.1.
DR   AlphaFoldDB; A0A077FIC1; -.
DR   KEGG; palk:PSAKL28_47040; -.
DR   eggNOG; COG4953; Bacteria.
DR   HOGENOM; CLU_006354_7_3_6; -.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000028931; Chromosome.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR011815; PBP_1c.
DR   InterPro; IPR009647; PBP_C.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   NCBIfam; TIGR02073; PBP_1c; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR   Pfam; PF06832; BiPBP_C; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   DOMAIN          57..223
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          299..416
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          690..773
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   777 AA;  85154 MW;  F65298C06905BF1C CRC64;
     MPILAKRLSV VSAVVLLCGA LLWAADRLWP LPLPADDLAR VVLAEDGTPL WRFADADGVW
     RYPVSADQVS PYYLQALLTY EDRWFYQHPG VNPLALVRAA WQNLRGGRVL SGGSTLSMQV
     ARLLDPHSRT VPGKLRQLWR TAQLEWHLSK AQILEIYLNR APFGGTLQGV AAASWAYLGK
     SPQHLTPSEA AMLAVLPQAP SRLRPDRHPA RAQVARDKVL KRLAEYQVWP QQRVIEAMEE
     PLLLAPRQEP ALAPLLARRL NRPHSPPLIR TTVDAALQRR LEDLLLGWRA RLPERTSAAI
     LVVEAQTMAV RAYLGSVDLN DERRFGHVDM ITALRSPGST LKPFLYGMAM DDGLIHSESL
     LQDVPRRYGD YRPGNFSMGF SGPVAASSAL ALSLNLPAVQ LLEAYGPKRF AAQMRNGGVP
     LTLPPLAEPN LSLILGGAGS RLEDLVAGYG ALSRGGMSAP MRLQPDAPLL EHRLLSPGSA
     WIIRRILSGQ ARPDRDPHAE LVQRPLLAWK TGTSYGFRDA WSIGVGPRYL IGIWIGRPDG
     TPVPGQFGLA SAAPLMLQVH DVLSNRDSQR GIAVPVAAVP ENVGVAAICW PLGQPLARQD
     SNCRRQRFAW TLDGTTPPTL QAADQPLSVG LRETVWVNTQ GQRVDASCPG AQAREVALWP
     APLEPWLPRV ERREARLPPV DPHCPPQVPA TAPPLSIVGV RQGDQLRRPA TSSEPLRLEV
     SALGGSGRRW WFLNGAPLGE SQGQEYLSAR FEQSGRVELS ALDESGQTAR VEFQINE
//
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