ID M7NKA5_9BACT Unreviewed; 801 AA.
AC M7NKA5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=mrcA_1 {ECO:0000313|EMBL:EMR02205.1};
GN ORFNames=ADICEAN_02644 {ECO:0000313|EMBL:EMR02205.1};
OS Cesiribacter andamanensis AMV16.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cesiribacteraceae;
OC Cesiribacter.
OX NCBI_TaxID=1279009 {ECO:0000313|EMBL:EMR02205.1, ECO:0000313|Proteomes:UP000011910};
RN [1] {ECO:0000313|EMBL:EMR02205.1, ECO:0000313|Proteomes:UP000011910}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMV16 {ECO:0000313|EMBL:EMR02205.1,
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:EMR02205.1}.
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DR EMBL; AODQ01000068; EMR02205.1; -; Genomic_DNA.
DR RefSeq; WP_009196034.1; NZ_AODQ01000068.1.
DR AlphaFoldDB; M7NKA5; -.
DR STRING; 1279009.ADICEAN_02644; -.
DR PATRIC; fig|1279009.4.peg.2681; -.
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 35..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..272
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 446..686
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 772..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 91101 MW; 141ECAFB0E6E90FA CRC64;
MKEEADLNQP QPLTFWQKAR IYLTERRYDF TRIPLANKIG VVLGLLVITT FMALFFFYQA
VRLEFFGEVP SKAELKDIRT SVASEVYSSD GKLLGRYFIQ ERTSTPYERI SPNIIKALIA
TEDARFYQHD GVDHKSIGRV IFKTLMLQEE SSGGGSTISQ QLAKNLYPRK RHRGRFLTLA
VNKMREMIVA ERLEDIYEKE DILELYLNTV PFSDNAFGIE TASERYFNKK ASQVNPQEAA
TLVGMLKATT SYNPRKNPQQ ATHRRNVVLG QMGKYGYLTA RQTDSLQATP LKLDFYQQSH
NEGLATYFRT HLAQELQRWC ANNTKPDGTP YNLYRDGLKI YTTLDSRLQE HAEKAVMDQM
KELQASFFAH WKGRAPWSGN TKILIKAVER SPRYRQLKAE GLETKEIQKV FAEKVPMKLF
TWKGEIDTLL SPLDSVKYYL YYLNAGFMAM DPHNGQVKAW VGGINHKYFK YDHVNNKTRR
QVGSTFKPIV YAAALQQGAD PCTYISAERE VYHDMDGWSP GNSDGNYEGE YTLAGGLMNS
VNTVSVKVIK RTGLSNVINL ARAMGIKNEI PKVPSIALGT AELSLYEMVA AYAVFANKGR
TIEPTYLLRI ENSQGEVLDV FAPEEQGRLA LEPDKADMML QMLRTVVNQG TASRLRWKYK
VNNDIAGKTG TTQSHADGWF IGISPDLVVG TWVGADDPGI RFRSINLGQG GSTALPIFAR
FWQEVNKDTT YTRLSEAKFK ISPQLLASMN CEPYRAPMDM DLFDRIFGGK DERDQRRQER
QQNQQQEEKK RGILKKIFGG G
//
