ID A0A1M5RAN7_9GAMM Unreviewed; 729 AA.
AC A0A1M5RAN7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN04488068_2989 {ECO:0000313|EMBL:SHH23228.1};
OS Hydrocarboniphaga daqingensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Nevskiales;
OC Nevskiaceae; Hydrocarboniphaga.
OX NCBI_TaxID=490188 {ECO:0000313|EMBL:SHH23228.1, ECO:0000313|Proteomes:UP000199758};
RN [1] {ECO:0000313|EMBL:SHH23228.1, ECO:0000313|Proteomes:UP000199758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7049 {ECO:0000313|EMBL:SHH23228.1,
RC ECO:0000313|Proteomes:UP000199758};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQWZ01000007; SHH23228.1; -; Genomic_DNA.
DR RefSeq; WP_245793297.1; NZ_FQWZ01000007.1.
DR AlphaFoldDB; A0A1M5RAN7; -.
DR STRING; 490188.SAMN04488068_2989; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199758; 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:UP000199758};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..729
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012793502"
FT DOMAIN 76..233
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 323..551
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 640..723
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 729 AA; 77951 MW; 34F9F7551C6F8DA8 CRC64;
MRSTWPAMPR RLTNRLLAAL ALLMAGSASL LAAAWLWDVT TPPAMPDPDA ARAAYRTSDA
VLLDRHGAPI QSLRIDLHGR RLEWTPLTDV SPALRAAVIQ AEDRRFEQHA GVDPLAVLGA
LRDRVSGRAR RGASTITMQL AAQLDPQLGG GRQRRSMLQK LRQMRAAQAI ETRWSKDQIL
EAYLNRAGFR GELQGIAAAS AALFGKQPAG LDADDAWTLA ALLPAPGAAP PAVAVRACRL
ARISGAACAA QQARTLAALA AQRSVGGTGA ADDTSLAPHL ARQLLRRAGE RVVSTLDAGV
QRLAQQALRT QLAGLGREQV RDGAAVVVDN ASGDMLAYVG SAGPASRAPQ VDGARALRQA
GSTLKPFLYA LAIEQRWLTA ASLLDDAPVA LEAGPGLYRP QNYEHDYKGL VSVRTALAGS
LNIPAVRTLL LTGVDRFRER LHDVGYVAGL TQPGDWYGYS LALGSADVSL LEQVNAYRTL
ARGGRWSPLR LRPSDPSPDP RPVIASEAAW IVRDILADRS ARAITFDLEG PLSTPYRASV
KTGTSKDLRD NWCIGGTQRY TVGVWVGNFE GDPMRTVSGI TGAAPAWREI LDALPRDDAD
TDAAPAGLVQ QALRYEAGIE PPRQEWFIAG TQTSQVAIAR PTAQRARLVS PATGSLIALD
PDIPLSRQHV PLQAQPASAS LRLRLDGRDI GSAAKVVLWT PLPGPHQLEL LDAEGRSLDR
VDFSVRRPG
//
