ID   A0A1H6RIX1_9LACT        Unreviewed;       863 AA.
AC   A0A1H6RIX1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SAMN04488113_10255 {ECO:0000313|EMBL:SEI52467.1};
OS   Alkalibacterium gilvum.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alkalibacterium.
OX   NCBI_TaxID=1130080 {ECO:0000313|EMBL:SEI52467.1, ECO:0000313|Proteomes:UP000198564};
RN   [1] {ECO:0000313|Proteomes:UP000198564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25751 {ECO:0000313|Proteomes:UP000198564};
RA   Varghese N., Submissions S.;
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};
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DR   EMBL; FNYW01000002; SEI52467.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6RIX1; -.
DR   STRING; 1130080.SAMN04488113_10255; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000198564; Unassembled WGS sequence.
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        40..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          97..284
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          423..662
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          799..863
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..863
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   863 AA;  96602 MW;  7014A3DA251450C0 CRC64;
     MKRSENEEHK QSEETKKSSY SALFQSFVHY FDIFYRVVKA LVILLIIVLL VVGSLGAGTA
     VGYFASLVHG SEPPKQEEMI SQIQDYTRKS NMYYADGSLI SEVRSDLLRT PVSLDNVSDF
     VINALVSTED EYFFEHEGVV PKAVIRALVQ ELSDSGATTG GSTLTQQLIK QQILSPEVTH
     ERKANEILLA YHLENKVDKE KILEAYLNVS PFGRNNKGQN IAGVEEAAQG IFGVSASEVS
     LPQAAFIAGL PQRPIVFSPY TQYGEIKENH ELSINRQNEV LFRMYREGHI SQEEYDEARA
     YDITQDFINK ENIEYNDNSY VYDIAYLQSL ELLTQKFMDA EEITDDMIEE NPDLVSKYQE
     RAEYALKNQG YKVYTTIDKD IHNTLERVTN EYVDKLGRER SYTYTDDEGE THTVTKPINT
     SGAMIDNQTG RVLGFIGGRD YDYSQFNVAF DGNRQPGSVI KPLAVYGPAL DENLITPATI
     IPDTPYTVPD WDPNIGGFVD KQIGNATRTT NEWMTARKAL TVSQNIPASK IWMELKDKYN
     PGSYIRRAGL GPEDIIDSDF DNASFALGGL SKGLAPVDLI SAFSSMGNDG VHNEPYVIER
     IENSKGDVVH ENKNEESRVF SPEANYLLVD MLRDVHVAGT ARGTMDSLPF NADWISKTGT
     TQDRVDIWYV AGTPRITFGT WIGYGTNEIE IGDDFGIHPS RRNRNFWSEL VSAVYEVKPD
     VFGANETFPK PANITTDSVI NATGMKAGTV KTPGGGDFNY SGPTHSEIFK KDNIPGSTIY
     DFAIGADDDE LLNFWGSKKP APAKEKSKDE DAEEDNDSEE EKSEDDEKKD SEEEKEEENE
     SSEESSDDEK PNDNDSDNSE DEE
//