ID A0A2S5A4J6_9SPHI Unreviewed; 780 AA.
AC A0A2S5A4J6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=C3K47_07015 {ECO:0000313|EMBL:POY37508.1};
OS Solitalea longa.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Solitalea.
OX NCBI_TaxID=2079460 {ECO:0000313|EMBL:POY37508.1, ECO:0000313|Proteomes:UP000236893};
RN [1] {ECO:0000313|EMBL:POY37508.1, ECO:0000313|Proteomes:UP000236893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR-AV {ECO:0000313|EMBL:POY37508.1,
RC ECO:0000313|Proteomes:UP000236893};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-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:POY37508.1}.
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DR EMBL; PQVF01000004; POY37508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S5A4J6; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000236893; Unassembled WGS sequence.
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:UP000236893};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 79..261
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 439..682
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 758..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 89534 MW; 98A48B07CFC7FEA5 CRC64;
MFNKIISSIK NFFKKINSFL PKNKFVKGFI YLITIIIVFF IAVDFNLFWL FGYSPGFKDL
KNPPLATASE LYSADSVLIG RYYTENRTPV QFKDLPDNLK YALIDTEDAR FYKHSGIDLR
SLFSSIFSTL SGDRRGASTI TQQLSKNLYQ TRRQKSFGLL THIPVIKTLI YKTKEWITAV
KLEMVYSKDE ILTLYLNTVP FGNNSFGIKV AANKYFNKQV NQLTPEESAV LVGMLKATST
YNPITNPVKS RERRNIVLSQ MVKYNHLPRP EYEKLLLTPI VLDLSYKEDN QQEKDSYVRN
AVANWIKDWA KENDYDIYAD GLKIYTTIDS RMQKYAEEAV EDRMAALQRR FYGYWQNRNP
WTDENGDEIP NYMETMVERL PVYKQLTKKY KGNIDSIDNA LNQKKRMTVF TWKGEKDTTF
STVDSMRYYS QILQTGLITI EPSTSRIRAW VGGINYDYFK FDHVIQSKRQ AGSTFKPFVY
LTAIDYKKMS PCDKIKDQPV TINYVENGEK KSWSPKNADW HFTGYDMTLR WALGKSCNSV
TAQLTQIVGW DNVVKYAHTC GIESPLKSVP SVGLGSNDVS LFEMATAYSV FLNKGMYAKP
LLVTRIYDKD GKLIKEFKPE PKRVLSEETA WLMVYMLQGG MQEPGGTSQA LWEYDLFKKG
NEIGGKTGTT SNYSDGWYMG VTKDLITGTW VGCEDRNIHF MSGEYGEGSK TALPIFGKYM
EKIYSDPTLG ITMGKFPKPD IKIQTKYYCP NSVPRRDTTS GIDSVNVEEE TLPDSIDTGF
//
