ID H8K8J3_RICAC Unreviewed; 784 AA.
AC H8K8J3;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=MC5_06740 {ECO:0000313|EMBL:AFC71586.1};
OS Rickettsia australis (strain Cutlack).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=1105110 {ECO:0000313|EMBL:AFC71586.1, ECO:0000313|Proteomes:UP000007589};
RN [1] {ECO:0000313|Proteomes:UP000007589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cutlack {ECO:0000313|Proteomes:UP000007589};
RA Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RT "Complete genome sequence of Rickettsia australis strain Cutlack.";
RL Submitted (FEB-2012) 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}.
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DR EMBL; CP003338; AFC71586.1; -; Genomic_DNA.
DR RefSeq; WP_014413108.1; NC_017058.1.
DR AlphaFoldDB; H8K8J3; -.
DR STRING; 1105110.MC5_06740; -.
DR KEGG; rau:MC5_06740; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_3_5; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000007589; 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: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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
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 Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..198
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 295..538
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 702..780
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 784 AA; 88541 MW; 362D03F44ECA9C56 CRC64;
MSLKTKLLFI TISGIIILYF AIPPAPLLKD ISFSQRVFDR SGELMRISLS KDDKYRIFTP
ICEIPASFIE AVLLYEDRHF YKHFGINPVS LAKAFYSTYL QNNRKIGGST ITMQIARLRY
GVNSSTILGK IHQIIKAIHV ELHYSKNEIL EAYLNLVPYG SNIEGITAGS YIYFNRDLKD
LNVLDILSLA VIPQNPLKRG GNDINIFKAR KYLFTEWLTT HPQDIIYNKL ISLPIKFNQN
KNLPFIAPHF TLDILANNDS PIIHTTIDKN LQTTIEKQVQ LYINNLKKYG INNASVILID
FTTMEVLASI GSGDFFNNDI CGQINGTKSH RSPGSALKPF VYALSFDQSL IHPLTLLKDT
PTYYDHYKPE NFDSRFTGGL SVRESLIKSR NVPVIFLASK LKNPNFYEFL QQAKISGLRK
PEHYGLSIVL GTAEITLEEL TTLYAMLANF GTYKPLRKML STSLRGEAKL GCDTLEQNNT
NSTRLPHSEQ MLATTMISPE ASYLTLDIIK DTTRPITYNN TKHNLPIYWK TGTSSSFRDA
LSVGIFGKYV LAVWVGDFKG QTHGTFTGNI SAAPLFFNVI ESIAQPNKDK DLILSKINEL
NITKVKVCAD TGDIDNDMCP VKAESLFIKG KSPIKQSGIY RKILIDLKTG MPACNFIQGQ
TEYKTVNLWP TDMLSVYQKA GIHILPKPIP TNHCNRLINW HHQKPKIIYP LRNSIHSIKD
SDNITFSAIS DNKTNNIFWF VDNELIATAK SNEPVIWKAK TGEFIIRAIS DSGENDSIKI
YIKE
//
