ID A0A248JT80_9PROT Unreviewed; 681 AA.
AC A0A248JT80;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpC {ECO:0000313|EMBL:ASG21809.1};
GN ORFNames=Y958_04435 {ECO:0000313|EMBL:ASG21809.1};
OS Nitrospirillum amazonense CBAmc.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Nitrospirillum.
OX NCBI_TaxID=1441467 {ECO:0000313|EMBL:ASG21809.1, ECO:0000313|Proteomes:UP000197153};
RN [1] {ECO:0000313|EMBL:ASG21809.1, ECO:0000313|Proteomes:UP000197153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBAmC {ECO:0000313|EMBL:ASG21809.1,
RC ECO:0000313|Proteomes:UP000197153};
RA Schwab S., dos Santos Teixeira K.R., Simoes Araujo J.L., Soares Vidal M.,
RA Borges de Freitas H.R., Rivello Crivelaro A.L., Bueno de Camargo Nunes A.,
RA dos Santos C.M., Palmeira da Silva Rosa D., da Silva Padilha D.,
RA da Silva E., Araujo Terra L., Soares Mendes V., Farinelli L.,
RA Magalhaes Cruz L., Baldani J.I.;
RT "Complete genome sequence of Nitrospirillum amazonense strain CBAmC, an
RT endophytic nitrogen-fixing and plant growth-promoting bacterium, isolated
RT from sugarcane.";
RL Submitted (JUN-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=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
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; CP022110; ASG21809.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248JT80; -.
DR KEGG; nao:Y958_04435; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000197153; Chromosome 1.
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:UniProtKB-EC.
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; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000197153}.
FT DOMAIN 48..214
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 291..518
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 592..678
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
FT REGION 221..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 71588 MW; 79507A6E7857BB3C CRC64;
MGAGVLALAL LVVALDRLFP PDLRRWQERS TLVTDEGGEV LRAFITADGA WRLPMSATEA
NPTYLAMLLA YEDHRFYHHP GVDPLALARA AGQALRHGRI VSGGSTLTMQ VARLLEPRPR
TVASKLLEMA RALQLEARYS KSDILGMYLT LAPFGGNLEG ARAASLAYFG RPPAALTPGQ
AALLVTLPQS PTKRRPDLAP AAARAGRDAL LRRMAAKGVL SRQAAREGMS EPLPTDRRPL
PFLAPHLADR LRRAAPPGSV IASTLDAGLQ RRVEATVRGT QDTLEPAAEV AVLVMEIGSR
KVRAYVGGSF SGPFGQVDMA AAPRSPGSAL KPFLYGLGFE ALPLHPETRI NDVPTVFGDY
APRNFDGGFH GLVTVREALQ QSLNVPAVKV LDRLGPARFL GRLREVGAQV VLPRPDAAPG
LPLALGGLGL SLADLTNLYA DLGDGGQARP LLLTPSEAPG PKRPAKRLMG AVAAWYVAEI
LSGTPRPDGR AAVGGRWVAY KTGTSYGFRD AWAVGFTSTH VVGVWVGRPD GTPRPGAAGR
DMAAPLLFRL VDLLPDWGTP PEPPPGVLEA GPGHALPPAL ALFDRGTPGG SLAAAAAPLR
IAFPPDGAEV ERTPGRDGAP VPVPLEALGG RPPLHWLGNG LPLPDSASGE GADWIPDGIG
FADIAVIDAA GQRAKATVRV R
//
