ID A0A845M348_9RHOB Unreviewed; 681 AA.
AC A0A845M348;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN Name=pbpC {ECO:0000313|EMBL:MZR13642.1};
GN ORFNames=GQE99_11500 {ECO:0000313|EMBL:MZR13642.1};
OS Maritimibacter harenae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Maritimibacter.
OX NCBI_TaxID=2606218 {ECO:0000313|EMBL:MZR13642.1, ECO:0000313|Proteomes:UP000467322};
RN [1] {ECO:0000313|EMBL:MZR13642.1, ECO:0000313|Proteomes:UP000467322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DP07 {ECO:0000313|EMBL:MZR13642.1,
RC ECO:0000313|Proteomes:UP000467322};
RA Kim J., Jeong S.E., Jung H.S., Jeon C.O.;
RT "Maritimibacter sp. nov. sp. isolated from sea sand.";
RL Submitted (DEC-2019) 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=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
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:MZR13642.1}.
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DR EMBL; WTUX01000012; MZR13642.1; -; Genomic_DNA.
DR RefSeq; WP_161351764.1; NZ_WTUX01000012.1.
DR AlphaFoldDB; A0A845M348; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000467322; Unassembled WGS sequence.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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:InterPro.
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; IPR050396; Glycosyltr_51/Transpeptidase.
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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000467322};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 66..224
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 304..525
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 599..677
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 681 AA; 71793 MW; F9D25894E5D6941A CRC64;
MRLWPGLLLV GALLSAAAGR DAVDDWVART ELPPLTVETS DEVLDRDGRL LRAYTVADGR
WRLGLDGAPV DPLFLDLLIA YEDKRFRRHH GVDPFAVARA AGQAVANGGV VSGASTLTMQ
TARLLEDGPT GTLPGKLRQV RVALALEQRL TKDEILALYL DRAPYGGNTE GIRAATRAWF
GKEPGRLTPA EAALLVALPQ SPETRRPDRH PEAARAARDR VIERTRAAGV LDPERAETAR
RAPVPTQRRA LPALAPHMAD RVRAEGPGPD GRLATTLDAG MQARLEALAR RAVADHGAGR
LSIAMVVADH RSGEVLASVG SAEYAPTDRQ GFVDMTRAHR SPGSTLKPLV YAMAFDDGLA
HPETMIDDAP IAFGSYTPEN FDGAFRGPVS VAEALRLSLN VPVVALASEI GPARILAALE
TAGAEPRLPG GAPGLAITLG GLGVRAEGLT ALYAGLASGG QVVELTHRPG TPRAVPGRLV
SPEAAWQVGH ILSGLAPPPN APRIRLAYKT GTSYGHRDTW AVGFDGRYVV TVWMGRPDGT
PVPGAFGAEM AAPILFEAFS RVTPDVAPLG PPPPGTLMLS HAALPRPLQS FRPRDAVFAA
PEGEPELAFP PDGALVETGG MPLAVKIRDG QPPFTVMANG APVLVQSHAR DTMLDLPAPG
HVTLSVIDAA GRAARAQVEL R
//
