ID A0A1I4ARC9_9PORP Unreviewed; 805 AA.
AC A0A1I4ARC9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-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=SAMN05216357_103213 {ECO:0000313|EMBL:SFK59082.1};
OS Porphyromonadaceae bacterium KH3CP3RA.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae.
OX NCBI_TaxID=1855396 {ECO:0000313|EMBL:SFK59082.1, ECO:0000313|Proteomes:UP000198708};
RN [1] {ECO:0000313|EMBL:SFK59082.1, ECO:0000313|Proteomes:UP000198708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH3CP3RA {ECO:0000313|EMBL:SFK59082.1,
RC ECO:0000313|Proteomes:UP000198708};
RA de Groot N.N.;
RL Submitted (OCT-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; FOSU01000003; SFK59082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4ARC9; -.
DR Proteomes; UP000198708; 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: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 Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..245
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 323..575
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 719..802
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 805 AA; 90556 MW; 7D2BB6D775F0D8EE CRC64;
MGEKLKGVVK KTGEWISLCM SRLLQWFYVL HLRKKIALLV LAFLLVWYLF SLPGTLFPSP
YSTLVSDRNG ELLGARIASD GQWRFPPADS VPGKYEICLI QFEDRHFRYH PGVNPLALGR
AMIQNVEAGR VVSGGSTITM QTVRLMRRNK RTYFEKFIEI ILATRLELSY SKKKILALYA
SHAPMGGNVV GIDAASWRYF GHSAESLSWG EAAVLAVLPN SPAMMHFGRD REGLLKKRNR
LLRQLLDDNT IDQTDYELAV SEPLPDHPHP LPQIAPHLVT QAFLRNPGNH IQSTVDKHLQ
MRAEEILDRW NTEFSQNGIF NLAALIVDLE TNEILSYNGN VGFRTNAYGS QVDIIQSPRS
TGSILKPFLY CAMLQEGVLL PTELLPDVPI NINGFAPKNF SLGYDGAVHA DEALARSLNV
PSVVSLRKYG VPKFYDLLKK SGLTTLNRPA DHYGLSLILG GTEGTLWDIA NAYARMAHTV
TDYNRDGTYY EWENFRLLRD DYQFGERNQD ESPLFNAGAA WLTLQALTNV NRPEELNWDF
VPSLRRVAWK TGTSYGFRDA WAVGVTPKYL VAVWTGNASG EGRPGLTGAR TSAQVMFDLF
NILPATRWFE TPYGELAEVA VCRESGQLKG MYCPENSIDT LLVPAKGLQG AVCSYHRRIH
LSEDGQYRVY EQCAGDRGIR SVSWFQLPPS WEWYYKQQHP GYRSLPPFSP ECASGNISDA
VMQFIYPYPG AILRITKQLD GSRGKAVFEL AHRNTSTRVF WHLGTDYLGE TSNIHQMELS
PDPGEHTLTV VDENGISLSI RFKVD
//
