ID A0A7T7XN12_9SPIR Unreviewed; 792 AA.
AC A0A7T7XN12;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-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:QQO09360.1};
GN ORFNames=JFL75_00100 {ECO:0000313|EMBL:QQO09360.1};
OS Breznakiella homolactica.
OC Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales;
OC Breznakiellaceae; Breznakiella.
OX NCBI_TaxID=2798577 {ECO:0000313|EMBL:QQO09360.1, ECO:0000313|Proteomes:UP000595917};
RN [1] {ECO:0000313|EMBL:QQO09360.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RmG30 {ECO:0000313|EMBL:QQO09360.1};
RA Song Y., Brune A.;
RT "Description of Breznakiella homolactica.";
RL Submitted (JAN-2021) 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}.
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DR EMBL; CP067089; QQO09360.1; -; Genomic_DNA.
DR RefSeq; WP_215626663.1; NZ_CP067089.2.
DR AlphaFoldDB; A0A7T7XN12; -.
DR KEGG; bhc:JFL75_00100; -.
DR Proteomes; UP000595917; Chromosome.
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:InterPro.
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:UP000595917};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 64..230
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 309..558
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 704..778
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 792 AA; 86558 MW; 886AE5CB92C434C6 CRC64;
MFPKNRGRRA VLIAAALAVF PACIFNVVLC ITAPSAAVLY EGRAPSTRIY DRSGVFLREV
VNERGERCNP VALSEISAVL INAVLTAEDA AFYNHGGINW FSVLRASIDN KRSGRTVSGA
STVTMQLARM VFSHPRDMEG KIRQGFDALR IERVLSKEKI LEEYLNRVPV APGCEGVEAA
SYRYFSKPAS ELELAEAALL AGMIQAPSLY DPVRDPENAQ KRRDWVLQRM YETRRISRED
FETAAAVPLP RERPEIPVKA GHFTDYLLAE TRRRGDIRSS LDWELQEAAQ NLAAQHTRRF
RGNGLTNAAV VVLDNATGTI RVMVGSKDWG MDESGYVNGA ASPRQPGSTL KPFAYALAFD
KGWTPASLLA DIETEYISND RTLYIPRNYS RNFRGPVLAK EALASSLNIP AIRLVRDLGL
AGFLDVLRNA GFSSLNQNAS YYGLGLVLGN GEVTLIELAA AYAALARNGL YIPPSVTEPE
KTESSGPIQY GITRANEQST RIFSPQAAWM VTSILSDEAM RVQSFGSDSP LVFGFPVAVK
TGTSSDWRDS WTVGYTEEFT VAVWSGDFES VSMNQVSGSS GAGILFSNIL HLLYDNSEFI
PALPETPPGI ETRIVCAESG GLPHEFCPRK LTVSVPQGTE IPGCAVHALV YVDPASGAVL
RTGNGAAPEY APVRLVYSLP PEYDVWLKEN GKFTIPAGTA SGTAVPGSLV ITKPRRGDIY
IIEPGYSAEN QTIELTAASE IRMTAIDWYL NDTLISRASW PYTVSWPLEK GRHVLTARSG
SSRSDPVEFE VR
//
