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Database: UniProt
Entry: R5LJ10_9MOLU
LinkDB: R5LJ10_9MOLU
Original site: R5LJ10_9MOLU 
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
//
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