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Database: UniProt
Entry: A0A223NY73_9SPHI
LinkDB: A0A223NY73_9SPHI
Original site: A0A223NY73_9SPHI 
ID   A0A223NY73_9SPHI        Unreviewed;       797 AA.
AC   A0A223NY73;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-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=MuYL_2916 {ECO:0000313|EMBL:ASU34803.1};
OS   Mucilaginibacter xinganensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1234841 {ECO:0000313|EMBL:ASU34803.1, ECO:0000313|Proteomes:UP000215002};
RN   [1] {ECO:0000313|EMBL:ASU34803.1, ECO:0000313|Proteomes:UP000215002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BJC16-A31 {ECO:0000313|EMBL:ASU34803.1,
RC   ECO:0000313|Proteomes:UP000215002};
RG   Henan University of Science and Technology;
RA   You X.;
RT   "Complete genome sequence of Mucilaginibacter sp. strain BJC16-A31.";
RL   Submitted (AUG-2017) 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; CP022743; ASU34803.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223NY73; -.
DR   KEGG; muc:MuYL_2916; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000215002; Chromosome.
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:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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; IPR011815; PBP_1c.
DR   InterPro; IPR009647; PBP_C.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   NCBIfam; TIGR02073; PBP_1c; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR   Pfam; PF06832; BiPBP_C; 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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215002}.
FT   DOMAIN          69..228
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          311..577
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          704..792
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   797 AA;  89885 MW;  208AC02FFE4B61E7 CRC64;
     MRLGSNRISF LIKKPKVIII LSFLSALFLL FWLCLPSPLF NSPTSYVIDD TDGQLLGASI
     ATDGQWRFPP NADVPEKFRQ CIITFEDKRF MHHPGFDLLA LGRAFRQNFQ SNKVTSGGST
     ITMQVIRLAT KHKRNIWNKV IEIFMAMRLE AGFTKNEILS FYASNAPFGS NVIGLDAASW
     RYFGRSPDKL SWGEMAAMAV LPNSPSLVHP GKNRATLLKK RNLLLDRLYR NGIIDSTTAA
     LAKFEPVPDR PMPLPQLAPH LLQRFKTDHQ INTNGDTRIK TSIRAALQQQ VNDILERHHQ
     VLKANDVNNI AAIVLDVETG ATLAYAGNIA HKEDPEMESD VDVINAPRSP GSTLKPVLYA
     SMLHDGLLLP NSLMPDIPTQ IAGYHPENFD LGYDGAVPAS KALSRSLNVP AVKMLQQFKY
     ERFYDVLQKM GVTTLKRPAD HYGLSLILGG GENTLWELTG IYADMARVLN HYQKYNGKYN
     PADYHNPVYK INTETKQPDL EKSGLLDAGS IFYTLQAMEE VMRPGEEMLW QQFSSSQRIA
     WKTGTSFGFR DGWAIGITPK YVVGVWVGNT DGEGRPNLTG ISTAAPALFE IFRLLPVTRD
     WFEMPVGEMV KIKVCHQSGY RAGEYCDDQD EMWVPKSGLK VAVCPYHQLV HLSWDEKWQV
     TGNCTPPNQI VNKHWFVLPP SMEYYYKTKN YQYRVLPPFR PDCVQAENSA PMEVIYPKDG
     AKIYIPLEAD GSRGRVIFNA AHRQKGVKIF WHLDNKYVGE TTDFHQMAVN PPPGKHVLTL
     VDENGNTVHI EFEILQK
//
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