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Database: UniProt
Entry: A0A1M7FZR0_9SPHI
LinkDB: A0A1M7FZR0_9SPHI
Original site: A0A1M7FZR0_9SPHI 
ID   A0A1M7FZR0_9SPHI        Unreviewed;       797 AA.
AC   A0A1M7FZR0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SAMN05216524_101785 {ECO:0000313|EMBL:SHM09513.1};
OS   Mucilaginibacter sp. OK098.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1855297 {ECO:0000313|EMBL:SHM09513.1, ECO:0000313|Proteomes:UP000184158};
RN   [1] {ECO:0000313|EMBL:SHM09513.1, ECO:0000313|Proteomes:UP000184158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK098 {ECO:0000313|EMBL:SHM09513.1,
RC   ECO:0000313|Proteomes:UP000184158};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FRCM01000001; SHM09513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M7FZR0; -.
DR   STRING; 1855297.SAMN05216524_101785; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000184158; Unassembled WGS sequence.
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}.
FT   DOMAIN          69..228
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          311..571
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;  89451 MW;  0BF0E44F96BF41F9 CRC64;
     MRPGLNRIKS YLKKPKVIII LAFLLTLFLL FWFCLPKPLF NSPTSYVIDD TDGQLLGASI
     ATDGQWRFPP NAEVPEKFKQ CIIAFEDKRF MHHPGFDILA LGRAIKQNFH SSKITSGGST
     ITMQVIRLAT RHKRNIWNKL IEMFMAVRLE AGYSKNEILS FYTSNAPFGS NVIGLDAASW
     RYFGRSPDKL SWGEMAAMAV LPNAPSLVHP GRNRAILLKK RNLLLDKLYH QGVIDSITAA
     LAKFEPVPDR PMPLPQLAPH LLERFKSDHQ TNTHGDTRLR TSIRSSLQQQ VNEILERHHQ
     VLKSNEINNI AAVVLDVETG AALAYAGNIA HPEDPEMESD VDVVDAPRSP GSTLKPMLYA
     SMLQDGLLLP NSLMPDIPTQ IAGYHPENFD LGYDGAVPAS RALSRSLNVP AVKMLQQFKY
     ERFYGVLQKM GITTLKKPAD HYGLSLILGG GENTLWELSG AYADMARVLN HYTKYNGKYD
     PTDYHNPVYS VSSRKNKPEF EKSGLLDAGS IYYTLQAMEE VMRPGEEMLW QQFSSSQRVA
     WKTGTSFGFR DGWAIGITPK YVVGVWVGNT DGEGRPNLTG ISTAAPALFE IFRLLPVTRD
     WFEMPVGEMV KIKVCHQSGY RAGEYCDDTD DLWVPKSGLK APVCPYHQLV HLSADGKWQV
     TGNCTPPNQI INKHWFVLPP SMEYYYKTKN YQYRVLPPFR PDCVQAENAA PMEVIYPKDG
     AKIYVPLEAD GSRGRVIFNA AHRQSGVKIF WHLDDKYVGE TKDFHQMALN PPPGKHVLTL
     VDGNGNTVHI GFEVLAK
//
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