ID Q2YAE4_NITMU Unreviewed; 1034 AA.
AC Q2YAE4;
DT 20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=Nmul_A0974 {ECO:0000313|EMBL:ABB74277.1};
GN ORFNames=SAMN05216403_102147 {ECO:0000313|EMBL:SEF49293.1};
OS Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=323848 {ECO:0000313|EMBL:ABB74277.1, ECO:0000313|Proteomes:UP000002718};
RN [1] {ECO:0000313|EMBL:ABB74277.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB74277.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of Chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 / NCIMB 11849 / C 71
RC {ECO:0000313|Proteomes:UP000002718};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC
RT 25196.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABB74277.1, ECO:0000313|Proteomes:UP000002718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25196 {ECO:0000313|EMBL:ABB74277.1}, and ATCC 25196 /
RC NCIMB 11849 / C 71 {ECO:0000313|Proteomes:UP000002718};
RX PubMed=18390676; DOI=10.1128/AEM.02722-07;
RA Norton J.M., Klotz M.G., Stein L.Y., Arp D.J., Bottomley P.J., Chain P.S.,
RA Hauser L.J., Land M.L., Larimer F.W., Shin M.W., Starkenburg S.R.;
RT "Complete genome sequence of Nitrosospira multiformis, an ammonia-oxidizing
RT bacterium from the soil environment.";
RL Appl. Environ. Microbiol. 74:3559-3572(2008).
RN [4] {ECO:0000313|EMBL:SEF49293.1, ECO:0000313|Proteomes:UP000236751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nl13 {ECO:0000313|EMBL:SEF49293.1,
RC ECO:0000313|Proteomes:UP000236751};
RA de Groot N.N.;
RL Submitted (OCT-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=2.4.1.129;
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; CP000103; ABB74277.1; -; Genomic_DNA.
DR EMBL; FNVK01000002; SEF49293.1; -; Genomic_DNA.
DR RefSeq; WP_011380322.1; NZ_FNVK01000002.1.
DR AlphaFoldDB; Q2YAE4; -.
DR STRING; 323848.Nmul_A0974; -.
DR KEGG; nmu:Nmul_A0974; -.
DR eggNOG; COG0744; Bacteria.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_012369_0_0_4; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002718; Chromosome.
DR Proteomes; UP000236751; Unassembled WGS sequence.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; 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; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:SEF49293.1}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002718};
KW Transferase {ECO:0000313|EMBL:ABB74277.1}.
FT DOMAIN 138..332
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 827..932
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 1034 AA; 117133 MW; 8AAC8E96CA24352A CRC64;
MLIPTLRRAL RFFTPRVLIL LFAALSVAVF LVYREIETSW YQAWRLSKLA GDLKWEIRSG
RDEDFTQLAL SQTGPYDIRL GYSSLPRLLQ NLEKHGFEVQ AQAHASRQMK DLVRRGVFVP
YREKSQAGLE ITGSNGQSLY RVSFPKRVYD KFESVPSVIT SSLLFIENRE LLDETRPKKN
PAIDWARLGR AILDKGIQVF NSDHDVPGGS TLATQIEKYR HSPNGLTLTS GDKFQQIASA
SVRAYLQGDN TLAVRKQIMV DYLNTVPLAG ALGFGETNGI GDALWAWYGL DFEETNRILN
WQYRNETEFA KAAGRYKHVL SLMIAQRRPS YYLLAGRQEL DELTDAYLRV LTQVKVIPPR
LRDAALRQPL RFRDAFKPEE IKDFSAQKAV NAARVRLASQ LGLQGLYDLD RLDLSVQSTL
DIELQKRTTE MLRQLRDPIN AVAAGLYGHR LLGKEDPSKI IYSFTLSELT PDGAKFRILA
DNFDQPLDIN KGTKLDLGST AKLRTLVTYL EIVEALHRKY AAWELKALRA EEVDPSDALS
RWAIDHLLHS GDKSLRSMLN AAMERKYSAN PYERFFTGGG QHVFHNFKPE DNYRIMSVRE
ATTNSVNLVY IRLMRDIVRY YMFQVGGSSA KILRDASNSD RGEYLRRFAD KEGRVFINRF
YLKYKDKSTD PREVSDIFFS SFRHTPRRLA AAYRYIYPAS SLVEFVAFMT PHLPRFKQLD
TYRLEDLYEA YAPGKYSLAD QGHIVTVHPL ELWLARYLIL HPAADYKEVI DASAGERIAV
YHWLFNTIHK NSQDVRIRGL LEVEAFLEIH RSWKRLGYPF DSLVPSLATA IGSSADHPAA
LAELMGVILN DGVRVPTLLI ERLRFAADTP FETIVEKKPL QGERVFSPEL AATVRSVLTK
VVAVGTASRL AHAMVEEDGS EILIGGKTGT GDHRHITFSS SGVIKESRAV NRSATFVFFI
GDRFFGTMTA FVPGVDAANY TFTSALSTQV MKKLVPVLKP LIDKPPSWPE STLAEDAIRK
ALPEEKEKLQ PTSS
//
