ID U2ZNX6_PSEA4 Unreviewed; 774 AA.
AC U2ZNX6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpC {ECO:0000313|EMBL:GAD63190.1};
GN ORFNames=PA6_020_00120 {ECO:0000313|EMBL:GAD63190.1};
OS Pseudomonas alcaligenes (strain ATCC 14909 / DSM 50342 / JCM 20561 / NBRC
OS 14159 / NCIMB 9945 / NCTC 10367 / 1577).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1215092 {ECO:0000313|EMBL:GAD63190.1, ECO:0000313|Proteomes:UP000016560};
RN [1] {ECO:0000313|EMBL:GAD63190.1, ECO:0000313|Proteomes:UP000016560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14909 / DSM 50342 / JCM 20561 / NBRC 14159 / NCIMB 9945 /
RC NCTC 10367 / 1577 {ECO:0000313|Proteomes:UP000016560};
RA Yoshida I., Hosoyama A., Tsuchikane K., Noguchi M., Hirakata S., Ando Y.,
RA Ohji S., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Pseudomonas alcaligenes NBRC 14159.";
RL Submitted (SEP-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD63190.1}.
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DR EMBL; BATI01000020; GAD63190.1; -; Genomic_DNA.
DR RefSeq; WP_021701277.1; NZ_BATI01000020.1.
DR AlphaFoldDB; U2ZNX6; -.
DR STRING; 43263.A0T30_05470; -.
DR eggNOG; COG4953; Bacteria.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000016560; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000016560}.
FT DOMAIN 60..208
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 302..550
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 684..765
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 774 AA; 85691 MW; 56707F31DD8D47BC CRC64;
MPALPFTSRR RHRLGLFVLA AASLLLALRL WPHTPLREAA PLSRMVLAEN GELLRMTLAS
DGQYRLWVPL ERIAPAMVEA LLLKEDRHFY RHPGVDPTAL VRAAMATYGG GMRQGGSTLS
MQLARRLYDL NSRQIPGKLQ QIALALWIEA RHSKHDILEA YLNLAPMGGN IEGVEAASRI
YFGKAAAQLS LSEALALAVI PQQPGRGQFG PALQRARLQL MAQWRREHAD DPRNEGLLEL
PLQARTRRQL AFRAPHLSEQ LLASHTDNEL HSTLDPRLQR RLEQLVSQFV DDRRKLGVRN
ATAILVDSRD QAVKALIGSA DYFDASIHGQ VNGVQARRSP GSTLKPFLYG LALDQGVIQP
MSILKDAPSA FGAFQPENFD GKFAGPLTAQ DALIRSRNVP AVWLTSQLRQ PSLHGLLQRA
GIKGLREEEF YGLALALGGG ELTPAELARL YLMLAGDGRL RPLRWTREER SGPGAQLLSP
QAAFMVRDML RHNPRPDGLP ADARGRDWPV AWKTGTSWGF HDAWSAGLVG PYVLVVWVGN
FDATPNPAFV GIKTAAPLFF RIADALPLAL PEERVPADRP PSGLTRVEVC AASGELPNRW
CPQTRKTWYI PGVSPIRVSD LHRPVMVDRL TGKAACPPFD PATSELQVFE FWPSDLQRLF
ADAGLPRRTP PDAQRDCQVQ AAIDTREAPR ITSPLTQVTY SLRLSQPQES ITLAAHAAAD
ARLLYWFADH TLVGQGTPQT ALQWRPERSG QYRIRVSDDQ GRSTSRALQV EFLP
//
