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Database: UniProt
Entry: A3K2N0_9RHOB
LinkDB: A3K2N0_9RHOB
Original site: A3K2N0_9RHOB 
ID   A3K2N0_9RHOB            Unreviewed;       678 AA.
AC   A3K2N0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 59.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SSE37_16543 {ECO:0000313|EMBL:EBA08439.1};
OS   Sagittula stellata E-37.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sagittula.
OX   NCBI_TaxID=388399 {ECO:0000313|EMBL:EBA08439.1, ECO:0000313|Proteomes:UP000005713};
RN   [1] {ECO:0000313|EMBL:EBA08439.1, ECO:0000313|Proteomes:UP000005713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E-37 {ECO:0000313|EMBL:EBA08439.1,
RC   ECO:0000313|Proteomes:UP000005713};
RA   Moran M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2006) 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}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EBA08439.1}.
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DR   EMBL; AAYA01000005; EBA08439.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3K2N0; -.
DR   eggNOG; COG4953; Bacteria.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000005713; 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:UniProtKB-UniPathway.
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   3: Inferred from homology;
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:UP000005713}.
FT   DOMAIN          60..229
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          303..516
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          597..672
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   678 AA;  72768 MW;  15230F33EB9B0758 CRC64;
     MPERRGLRRL SALVVALWCV GFAGDRLSDW INATEIPLLV HATSPEVRDR NGDLLRAYTI
     DDGRWRMTVT PDQVDPLFYR MLIAYEDKRF FTHNGVDLQA AARAVAQGLR HGRVVSGAST
     LTMQVARLLE DGTTGQWQGK VRQMRLALAL EKRLTKDEIL ALYTLLAPYG GNVEGLRAAS
     LIWLGKEPRR LTPAEAALLV ALPQAPESRR PDRHPEAARE ARNRVMVRMA EAGVIPMSAA
     RSDALDPSPR GRFPMPQLAP HMADRAVAEA PGRHDLTLDA DLQRSLEDLA RRHMARLDPR
     LSMAIVLADH ESGEVLASVG SPDYAGTLNQ GFVDMTTAQR SPGSTLKPLV YALAFDRGLA
     HPETLILDTP VHFGTYAPQN FDGEYRGELT VRRALQLSLN IPVVRLTEAL GPAHLMAALQ
     GAGLKPALQG GTPGLALSLG GVGLTLEEMV QLYAALAHGG EARPLRWKAS TAEEATPRRL
     VSRASAWQVG HILAGITPPS AAGPKGRIAW KTGTSYGHRD AWALGWDGRY IAGVWIGRPD
     GTPVPGAFGA GLAAPVLFEA LGRVSARPVP LPAPPPETLM ISNAQLPANL QRFGPRAETV
     ALQVTFPPDG ATLAVSPSGV PLKLRGGTPP YTVLADGAVL ATGLRRPELL APISGPGFTT
     LSVIDARGQS GRTTIELR
//
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