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Database: UniProt
Entry: A0A2R3Z3Q2_9FLAO
LinkDB: A0A2R3Z3Q2_9FLAO
Original site: A0A2R3Z3Q2_9FLAO 
ID   A0A2R3Z3Q2_9FLAO        Unreviewed;       770 AA.
AC   A0A2R3Z3Q2;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=C7S20_06205 {ECO:0000313|EMBL:AVR44891.1};
OS   Christiangramia fulva.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Christiangramia.
OX   NCBI_TaxID=2126553 {ECO:0000313|EMBL:AVR44891.1, ECO:0000313|Proteomes:UP000241507};
RN   [1] {ECO:0000313|Proteomes:UP000241507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH35 {ECO:0000313|Proteomes:UP000241507};
RA   Hwang S.H., Hwang W.M., Kang K., Ahn T.-Y.;
RT   "Gramella fulva sp. nov., isolated from a dry surface of tidal flat.";
RL   Submitted (MAR-2018) 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}.
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DR   EMBL; CP028136; AVR44891.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R3Z3Q2; -.
DR   KEGG; grs:C7S20_06205; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000241507; Chromosome.
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; 2.
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:SF11; PENICILLIN-BINDING PROTEIN 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   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:UP000241507};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          70..245
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          429..687
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   770 AA;  87201 MW;  144CD62360F4DA06 CRC64;
     MAQKSKKTKK STHSNRPYII GFWTLFGIGI LLAIFVFLLA GWGAFGKMPT FEELENPETN
     LATEIFSSDG KTLGKYYNEN RTPVKYEDLP EHLVQALVAT EDERFYKHAG IDARGTLRAA
     VFLGQRGGAS TITQQLAKQL FTENVSDSFT ERIFQKIKEW VIATRLERQY TKEEIITMYF
     NKYDFVYQAV GIRSAAKIYF GKEAKDLNIQ ESAVLVGMLK NAALYNPVRR PDLVEARRNQ
     VLEQMNRNGY ISENEMDSLQ KLPMKIEFTP EGHDEGMATY FRAYLQGFMK DWIEKNPKPD
     GSHYSLYRDG LKIYTSIDSR MQGYAENAVK KHIAHLQEEF DRQNKNNPTA PFRDIDKSEE
     ENIIQQAMRR SDRWYTMKAE GKSEKEILAS FKKPREMRIF SWKGDIDTTM TPRDSILYYK
     SFLQAGLMSM EPQTGEVKAW VGGTNFKHFK YDHVKQGKRQ VGSTFKPFVY ATAIDQLKFS
     PCDTLPMSRF TIEAGKYGNM KDWSPQNAGN EGYEGMVTLK EGLAKSINTV TARLIDKTGP
     QPVIDLAQKL GVDVSNIPAV PAIALGVADI SLFEMVSAFS TFANQGVYVK PVVVNRIEDK
     NGTVLYQHTP VTRDVLSKEA AYVTINLLEG VTEAGSGVRL RGTWGKDRID YKRAVTGYPY
     DFKNPIAGKT GTTQNQSDGW FIGMVPDLAT GVWVGGEDRS VHFPTITYGQ GATMALPIWG
     MYMKDVYADD KLEVSKEEFE KPEDLSIEIN CDNYGRKKTS QSSVPDELDF
//
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