ID R5LJ10_9MOLU Unreviewed; 974 AA.
AC R5LJ10;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BN801_00419 {ECO:0000313|EMBL:CCY79140.1};
OS Mycoplasma sp. CAG:877.
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=1262907 {ECO:0000313|EMBL:CCY79140.1, ECO:0000313|Proteomes:UP000018280};
RN [1] {ECO:0000313|EMBL:CCY79140.1, ECO:0000313|Proteomes:UP000018280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:877 {ECO:0000313|Proteomes:UP000018280};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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 -!- 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:CCY79140.1}.
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DR EMBL; CAYV010000024; CCY79140.1; -; Genomic_DNA.
DR AlphaFoldDB; R5LJ10; -.
DR STRING; 1262907.BN801_00419; -.
DR Proteomes; UP000018280; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF29; PENICILLIN-BINDING PROTEIN 1A/1B; 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 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:CCY79140.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000018280};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 147..331
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 422..701
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 108518 MW; 53C26884A424FA4C CRC64;
MQKKEIKGRR PNNKKVTTKK STNTKNIKKR IVTNPKEDNQ IKLILLISFI AIVLLSYFTL
GTFFALLTGF GIGIIVGVAK LLDKCKEGKK TKKIIKIILM VILSIGIVCL VGFTIFLIFI
KINADPKYVT SKLETQENSE FLDINNEVYA KLGSEMREKV TYDELPEVLI DAIIATEDSR
YFQHNGFDAP RFIKASMGQV MQKLLHKGSN AGGASTLTMQ VVKNSLTNAY ATKGTEGIIR
KFEDIYLAIF KLEKDFTKEQ IIEYYVNNHY LGGNYYGVQE ASEAYFGKSV SELNLSEAAT
LAGMFKSPIY YSPTVYPEHA ETRRKTVLYL MKRHGYITEE EEKIANSIPI SSLTSEGGTT
QNNKYSGYVD TVVEELDTKY GINPYTTPVI VHTNLDRSKQ DGVNSVMNGE SYTWINDKVQ
AGVAVLDSQT GKILAIGNGR NIGDRSANKK GQWNYATKNK RQPGSTAKPL FDYGPGIEYN
NWSTYTLFED EPYTYSNGRS IQNWDGGYLG TLTLRKSLAY SRNIPALKAF QQVDNKKILE
FVSNLGMTPE VCSTGYTYNP NTMKCISKDG KSTEDPTRIH EAHSIGAFTG TNPLQMSAAY
AAFSNGGYYN EPYSVSKVVY KSNNETKEHN SDNYVVKRKA MSEATAFMIS SVLQDVTLNG
GNPVNVARKT GTTNYDSSTM ESKNLPWDAI RDSWIIGYST KTVVGLWYGY DFIDSEYCLH
NVPASVQKDK IFNALVNSGA MESNREAFKQ PDSVVKVGVV MGSNPPKLAG TYTGNVVYEY
FKKEYAPEET YVEEKLAAPE DFEATYNRLT KKVNLSWKAV STSGIDDENY GTFGYNVYFG
STLIGFTEKT SFTYTPTSSP YGTYKVVATY KSYSGIKSES ATYKLEEETT DNLELQYTGS
TTIPALTGAL TLSTSDFVVK NNGSTVSATI EQCTPNEIKL TGRQTITCTI KYKNKTETLT
TTINVTKEQE SETQ
//