ID A0A366XXS7_9BACI Unreviewed; 654 AA.
AC A0A366XXS7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=DS031_15030 {ECO:0000313|EMBL:RBW68751.1};
OS Bacillus taeanensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=273032 {ECO:0000313|EMBL:RBW68751.1, ECO:0000313|Proteomes:UP000253314};
RN [1] {ECO:0000313|EMBL:RBW68751.1, ECO:0000313|Proteomes:UP000253314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030017 {ECO:0000313|EMBL:RBW68751.1,
RC ECO:0000313|Proteomes:UP000253314};
RA Liu R., Huang Z.;
RT "Lottiidibacillus patelloidae gen. nov., sp. nov., isolated from the
RT intestinal tract of a marine limpet and the reclassification of B.
RT taeanensis BH030017T, B. algicola KMM 3737T and B. hwajinpoensis SW-72T as
RT genus Lottiidibacillus.";
RL Submitted (JUL-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}.
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:RBW68751.1}.
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DR EMBL; QOCW01000017; RBW68751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366XXS7; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000253314; Unassembled WGS sequence.
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; 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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000253314}.
FT DOMAIN 33..206
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 296..572
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 654 AA; 73189 MW; B7ADA5DA55996B98 CRC64;
MLGSLLMYVK LSGPPPLRVT QTTTFYGSDQ SIIGEKHQNG QNRYWVGLDD ISENVIHATI
AIEDRKFYDH NGFDFKRIAG AIIADIKAMA KVQGASTITQ QYARNLYLGH DKTWKRKAVE
ALYTMKLEMN YPKDKILEGY LNTIYYGHGT YGIEAAANYY FNKTAAELTL AEASILAGIP
KGPAYYSPYL NQENAENRQD IILSSMEKMN FITEAEKKDT LKETLTFVSH DQPKEKVAPY
FLDEVKKTVA QQLNLDPEAS EAGGLNIYTT LDPVLQEKAE KWVETTIGKE SELEAALVAI
DPRNGEIKAL VGGRDYQKSQ YNRATQARRA PGSTFKPFLY YAALQKGFTP STLLRSEKTT
FRYNDDKETY TPHNYGNHYA NDFITLAQAL ALSDNVFAVK THMLLGLDEL INTAKVFGIN
SPLAELPSLA LGTKPVGILE MTNAYSIFAN GGFQVPPSFV TKVTDHVGNV LYERELTRER
VIDKKSAFVM THLMTGMFDE NLNDYAGVTG ANIKNFLHRP AAGKSGTTSM DSWMIGFTPQ
LVTGVWIGYD QGKTLDNMSG KYAKKIWAQF MEDALQDKPA ASFKPPKGVV GVMVNPDNGL
LASEGCPVQR LTYYIEGTEP TEYCEEHIHE EPLPEEKAPK KEKGWLKRLL PWFN
//
