ID A0A2S7UXX6_9GAMM Unreviewed; 815 AA.
AC A0A2S7UXX6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 18-JUN-2025, entry version 28.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=BTO11_13460 {ECO:0000313|EMBL:PQJ54555.1};
OS Psychrosphaera saromensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Alteromonadales; Pseudoalteromonadaceae; Psychrosphaera.
OX NCBI_TaxID=716813 {ECO:0000313|EMBL:PQJ54555.1, ECO:0000313|Proteomes:UP000239007};
RN [1] {ECO:0000313|EMBL:PQJ54555.1, ECO:0000313|Proteomes:UP000239007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4-48 {ECO:0000313|EMBL:PQJ54555.1,
RC ECO:0000313|Proteomes:UP000239007};
RA Yoshizawa S., Kogure K.;
RT "Diversity of luminous bacteria.";
RL Submitted (DEC-2016) 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:PQJ54555.1}.
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DR EMBL; MSCH01000003; PQJ54555.1; -; Genomic_DNA.
DR RefSeq; WP_105053075.1; NZ_BMYG01000001.1.
DR AlphaFoldDB; A0A2S7UXX6; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000239007; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000239007};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..216
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 311..565
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 726..809
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 815 AA; 91706 MW; 5419B31B166DE20C CRC64;
MSSRLNRKGF LLFRKAVLIA ALFMVLLYLF IPKPDITQHV SYSTAFYDND EKLLRLNLAT
DDRYRLWTPI DKIPLDIQEA TLLYEDQYFY QHIGINFVAL TKAFYTSYIK RSRRVGASTI
TMQLARLRYG MNTHVIVGKL EQIFRALQIE RHYSKKQILE AYFNLAPYGS NIEGVGAASL
IYFDKPASKL NLPESLLLSL IPQNPTKRNP IKKTAKPVLL DTRQKLFNRW LESHPEDADW
ASAMQLPISV QSTSDLPFLA PHFINHLRSE YPNLKSGQYK TSINLNLQKL LERHAQSYIQ
RRDRDGLNNT SALLLNYKTM EVVAELGSVD FFNRKISGQV NGTLAKRSPG STLKPFIYGL
AIDEGLIHPL SLVKDAARRY GAYTPENYDQ GFLGPITATE SLVLSRNVPA VNLMYELKKI
GLYDLLVAGG VKDLKPKEFY GLALALGGNE VTMLELVRLY AMLANFGVYK EEVILTPDPS
AVVSNQSTTE TEIDQYFLSN ANNNNNNNGS EPTSDENRLL SPEAAYLTLQ MLKQNTAVDE
MEFQKETRQE YPVYWKTGTS FAFRDAWSVG VAGPYVLAVW VGNFTGEGHP SFIGGTAAGP
LFFEIIRSLE SYGLIKDNLS ADGLNITDVD ICSSTGDLPN LHCPKTKKGL FIPGKSPIKI
SDVHREIYID KKTGLRACRF DAAITKKDVY EFWPSDLVTL FRQAGVVKRQ PPIYLESCDI
NETGTRGLAP TITSPSSLIS YTVRASKLKD EVLPFIATTD SDSHSLFWFI DNRFVGKVAR
DKPFFWHPEV GTFDVKVVDD LGRGSSTKVR VNLIQ
//
