ID M7NRF7_9BACT Unreviewed; 780 AA.
AC M7NRF7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=mrcA_4 {ECO:0000313|EMBL:EMR01099.1};
GN ORFNames=ADICEAN_03770 {ECO:0000313|EMBL:EMR01099.1};
OS Cesiribacter andamanensis AMV16.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC Cesiribacter.
OX NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR01099.1, ECO:0000313|Proteomes:UP000011910};
RN [1] {ECO:0000313|EMBL:EMR01099.1, ECO:0000313|Proteomes:UP000011910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMV16 {ECO:0000313|EMBL:EMR01099.1,
RC ECO:0000313|Proteomes:UP000011910};
RX PubMed=23682146;
RA Shivaji S., Ara S., Begum Z., Srinivas T.N., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cesiribacter andamanensis Strain AMV16T, Isolated
RT from a Soil Sample from a Mud Volcano in the Andaman Islands, India.";
RL Genome Announc. 1:E00240-13(2013).
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:EMR01099.1}.
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DR EMBL; AODQ01000146; EMR01099.1; -; Genomic_DNA.
DR AlphaFoldDB; M7NRF7; -.
DR STRING; 1279009.ADICEAN_03770; -.
DR PATRIC; fig|1279009.4.peg.3814; -.
DR eggNOG; COG5009; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000011910; 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:UP000011910};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..271
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 445..686
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 780 AA; 87721 MW; B24223A440FF46BB CRC64;
MGATTLVKKR KKKQGSSRSA ATLYRKLVIG LWAGFVALLL GFPLYLYTVS VDFLGLFGGM
PSATMLENAE NDLASELWGA DGKLLGKYFR ENRENAAYDE ISPYLVHSLK AVEDARFEEH
SGLDGVSLIR VAIKSVLLGQ NKGGGSTLSQ QTAKVMFDLR TDEQYEGKLH GINYKLDMLL
KKTKEWILAV QLERTYTKKE ILALYLNTVS FGNNTYGVKV ASKVYFDKTP NSLNLQESAL
LAGVVQNPTR LNPVRQPENA LHRRNVVLHQ MVKYGYLTEA QFDSVKLLPL KLEYRIENHN
EGPAPYFRSV IREFLSKWAR ENGYNIYKDG LKIYTTIDSR MQRHAEQVVA SHMASLQTRF
EEEWRGRNPW IGEDGREIRG FLEQEIKKTE HYRKLVRKYG AKSDSVWIVL KTKRPMRVFS
YKGEKEMNLS PLDSLAYYKR FLHAGFMAMD PATGAIKAWV GGVNHTHFKY DHVQQGKRQP
GSTFKPFVYA TAIENGYSPC YQVYDVPRSY ETGSGTPWEP KNSDGKWTNA PMSLREALAR
STNSVTAEMM HKMKPENVVA MARRMGISSE LEPVLALSLG VNDVSVHELV GAYSTFVNRG
VYTQPYYITR IEDKNGNLLY KPEPVTREAL NEETAYLMLH MLSGGAEMGI GSSARLSPSL
LQRVAVGAKT GTTQNGSDGW FMGVTPELVA GAWVGGDSRH IRFPSWTSGQ GARTAMPIWD
QFMVRVMNDK ALGFKKTAFS MPEKPLTIET NCDRYGRGTT DSDSVEVAPR PVISPDDVMF
//
