ID A0A2Z4GBW8_9BACT Unreviewed; 833 AA.
AC A0A2Z4GBW8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=DJ013_11630 {ECO:0000313|EMBL:AWV98789.1};
OS Arcticibacterium luteifluviistationis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Arcticibacterium.
OX NCBI_TaxID=1784714 {ECO:0000313|EMBL:AWV98789.1, ECO:0000313|Proteomes:UP000249873};
RN [1] {ECO:0000313|EMBL:AWV98789.1, ECO:0000313|Proteomes:UP000249873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1504 {ECO:0000313|EMBL:AWV98789.1,
RC ECO:0000313|Proteomes:UP000249873};
RA Li Y., Qin Q.-L.;
RT "Complete genome sequence of Arcticibacterium luteifluviistationis SM1504T,
RT a cytophagaceae bacterium isolated from Arctic surface seawater.";
RL Submitted (MAY-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}.
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DR EMBL; CP029480; AWV98789.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4GBW8; -.
DR KEGG; als:DJ013_11630; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000249873; Chromosome.
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:UP000249873};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 52..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 106..285
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 481..720
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 833 AA; 93385 MW; 359A82AC0D70DB73 CRC64;
MIKEIFTKVK ENKYVQKFSK ASRVLFGKVL KFSVFNRSEF KSATLLSKVF RLTYTFGLLL
VTFVFALESN FLWLFGDMPT MKEARNTKLA VPSEIYSSDE KLLGLFYVEN RSPIPFEEID
SLTVKALIST EDARFYLHNG LDIVSLSGAV FSTLTGDKRG GSTIHQQLVK NIYNTRHVNS
RGLLAYIPGL STLVAKIKEW DTAIKLDWFF EKNEILALYL NAVDFGDNTF GIKLASEHFF
SKKPQDLELH ETALLIGILK GTNYYSPKRR PERALARRNV VLEQMLKYND IDSLAFENAI
KKPLGLKITE INKEESSAPY FRTMLRPLLI AWCEENGYSL FSDGLKIYTT IDSRMQTNAE
EAVKSHLTEI QRSLDLEQGS YKYWFKKKIA EEKAAFKREN PRVKDIPEMP TEVVLNKLVK
QSGSYKNFRS AGLTEEEALE AMNKPHQTVL ATHTGEKKMT ISALDSIMYM SQFLQAGLLS
IDPTNLHVRA YVGGSNYDYF KYDHVVQAGR QPGSAFKPII YASALENGYP ACTTIIDKPF
SIETSIGGKQ TTWAPKNSNG TYTYAPVNLR RALGTSINSI AIRVLQDVGT DKVIKTAEKL
GIQSKLDNNL SLALGTSNVT LLELTRAYLP FANQGMSGDV VLFDKIIDKT GEVVFEHKPD
LKQVLAPEKA YEMSYLLRGA VEEGGGTARR LYNYGIPYGN EIGGKTGTTN DYVDAWFMGV
MANLVTGVWV GCDDSRIHFT SGNGAGGRAA LPIYGKFLQA SYADKKIGLE KTTFTKPEDY
DSALLNCHFV PVVEDSTATD SLAVNQDSLM IQRRDEFRAL DVETIEIKQP TLE
//
