ID   U5S852_9LACT            Unreviewed;       943 AA.
AC   U5S852;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=Q783_02760 {ECO:0000313|EMBL:AGY81221.1};
OS   Carnobacterium inhibens subsp. gilichinskyi.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1266845 {ECO:0000313|EMBL:AGY81221.1, ECO:0000313|Proteomes:UP000017469};
RN   [1] {ECO:0000313|EMBL:AGY81221.1, ECO:0000313|Proteomes:UP000017469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WN1359 {ECO:0000313|EMBL:AGY81221.1,
RC   ECO:0000313|Proteomes:UP000017469};
RX   PubMed=24285647;
RA   Leonard M.T., Panayotova N., Farmerie W.G., Triplett E.W., Nicholson W.L.;
RT   "Complete Genome Sequence of Carnobacterium gilichinskyi Strain WN1359T
RT   (DSM 27470T).";
RL   Genome Announc. 1:e00985-13(2013).
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};
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DR   EMBL; CP006812; AGY81221.1; -; Genomic_DNA.
DR   RefSeq; WP_023177137.1; NC_022606.1.
DR   AlphaFoldDB; U5S852; -.
DR   STRING; 1266845.Q783_02760; -.
DR   KEGG; caw:Q783_02760; -.
DR   PATRIC; fig|1266845.5.peg.493; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_2_0_9; -.
DR   Proteomes; UP000017469; Chromosome.
DR   GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.12800; -; 1.
DR   Gene3D; 3.90.1310.40; -; 1.
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:SF32; PENICILLIN-BINDING PROTEIN 2A; 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   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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        99..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          155..342
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          498..772
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          55..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          890..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   943 AA;  104444 MW;  9014614F4A33B0EE CRC64;
     MNSPQNNNEP TFFKKLKVSL KKVLPFIKNK WISFKTIILK QSVILKESLS RKDQSQINST
     SDSQSDNDQK RTQSKNVQKP ALDKVLFGFN VGYSVIKNLI LTIVVIGLIG AALAGGLGIG
     YFAYLVSGEE IPTYEEMKAD IENVSTTSAM YYATGEKISD LKTDLKRSEI PLSEMSPLVQ
     EAIIATEDEY FYKHSGVVPK AVARALVQEV TGASTTSGGS TLTQQLVKQQ ILTNEVSFKR
     KANEILLAFR VENYFTKEEI LENYLNVSPF GRNNKGQNIA GLNEASIGIF GVKANELTLP
     QAAFLAGLPQ NPIVYSPYTQ TGTLKEDLAA GMSRKDEVLF RMYRENYITK EEYDTAVAYD
     LTQDFLPQET DVKDSTDYVY NFVEQQARQI IMEQLYTADG YSAEDLSNDQ ELSDMYYNQA
     DQDLRMNGYT VYSTIDKGVY EAMNDVVEQY ANPEISYDEN NNPIINNTSY LGNVKVADYI
     DEETNETKTL VEPVQNGAVL RDNATGRIIS FIGGVDYEFT QVNHAYQSPR SPGSTIKPLL
     AFAPALEEGI ITPATMLFES SAKVPSWENG SLGIHEITNV GNVIPNKWTD VRTGLTQSSN
     IVTSKIYQQM KDTYHMEEKL ESYMHKMGFG SDVITTEEYQ GVYYALPIGG ITKGTTVLGQ
     TDGFSTLANK GNYTEGYIIE KIEDHTGNVI YQHEVEPVEV FSAETAYLTT DILRDVLESG
     TAKDIKGQLN FNADIAGKTG TSDGQKDIWF IGYTPQVTLS SWIGYDNAVN TSVNDLSNSG
     SESPSLRNRR HWARLMNAIY NANPTILGTD QTFQQPDGIV EAKVLAATGM QPGKVKLANG
     KEVTVSGATK TEIFNKKFVP KTTTYDFGFS ATDKELADYW GKASKTASDA AAKKAKAEAD
     KKTAEAKKAE ETKKAEETKA KAEKDKKAQE EAKKKAEEAK KNE
//