ID A0A1Y0I2K1_9GAMM Unreviewed; 823 AA.
AC A0A1Y0I2K1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 18-JUN-2025, entry version 32.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=OLMES_0625 {ECO:0000313|EMBL:ARU54728.1};
OS Oleiphilus messinensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Oceanospirillales; Oleiphilaceae; Oleiphilus.
OX NCBI_TaxID=141451 {ECO:0000313|EMBL:ARU54728.1, ECO:0000313|Proteomes:UP000196027};
RN [1] {ECO:0000313|EMBL:ARU54728.1, ECO:0000313|Proteomes:UP000196027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ME102 {ECO:0000313|EMBL:ARU54728.1,
RC ECO:0000313|Proteomes:UP000196027};
RA Kozyavkin S.A., Slesarev A.I., Golyshin P.N., Korzhenkov A.,
RA Golyshina O.N., Toshchakov S.V.;
RT "Genomic insights into alkan degradation activity of Oleiphilus
RT messinensis.";
RL Submitted (MAY-2017) 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; CP021425; ARU54728.1; -; Genomic_DNA.
DR RefSeq; WP_087459899.1; NZ_CP021425.1.
DR AlphaFoldDB; A0A1Y0I2K1; -.
DR KEGG; ome:OLMES_0625; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000196027; Chromosome.
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:UP000196027};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..236
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 312..537
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 701..785
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
FT REGION 790..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 90880 MW; 3282223106ABCEB3 CRC64;
MNSTRGFLKA GGLRRSARLL RIATPIMLMA LVLIVLDRCF PLNLPQHQRH FAQVVTDRDG
IPLRRFADDK GVWRYPTHLD AVSPRYIEAL LGYEDRWFYY HPGVNPIALV RAFLQNVQGG
KIVSGGSTIT MQVARLLHPH PRSVPGKLSQ ILRAIQLEWH LDKQEILALY LNNAPFGGTL
EGVEAAAFGY FNKSAAQLSH AEAALLAVLP QAPSRFRPDR HPGRAEQARN KVLQRLGEFQ
IWTEQTVLEA RQEKVAAFGL QSPQLAPLLA RRLMQDNPEP LLQTTLEFNL QQRVQDYVKL
YTAQLPAHSS VAVLIVENQN MEARAYVGSG QFGNTQRFGY IDMVTADRSP GSTLKPFLYG
MAIDAGLIHS HSLLTDTPRS YGLYQPDNFS GGFNGPVSAT AALQKSLNIP AVDLLARLGP
KTFVSRLQHI GIPLTLPNHE APGLALILGG TGTSLEALVS GFASLARGGL VAPVRYQHHE
PLKNRRLFSE GTAWVIHRIL QDSPHPDQLR TRRARGSNTD NPGIAWKTGT SYGYRDAWSI
GVSSDYTIGV WVGRPDGAPV PGHFGAVTAT PLMFTLFKQM PARRTTITRP GTVTDVEICW
PTGTKKVDTR PNHCHKTLTS WSVDKQVPPT YALAQENQVD RSPLTTIWIN PETGLRVDQN
CVNIKRVKRR VALWPGIVEP WLPAEQKRGQ QVPPLDPRCE QPAELSGQSL VIHKPETDTL
IQPPPGSNEL PTIALSTLGG IEHIGWYVNG QLWKQTAPNQ SVAFKPEHPG KFEFVAVDGS
GNTDRRILYF TSSRRPAPKP GSDISLRSSV ESPALSEPKP ESG
//
