ID A0A494XXP2_9BACL Unreviewed; 1032 AA.
AC A0A494XXP2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=D7Z26_09100 {ECO:0000313|EMBL:RKP55344.1};
OS Cohnella endophytica.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=2419778 {ECO:0000313|EMBL:RKP55344.1, ECO:0000313|Proteomes:UP000282076};
RN [1] {ECO:0000313|EMBL:RKP55344.1, ECO:0000313|Proteomes:UP000282076}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2MS4P-1 {ECO:0000313|EMBL:RKP55344.1,
RC ECO:0000313|Proteomes:UP000282076};
RA Tuo L.;
RT "Cohnella sp. M2MS4P-1, whole genome shotgun sequence.";
RL Submitted (OCT-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 -!- 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:RKP55344.1}.
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DR EMBL; RBZM01000004; RKP55344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494XXP2; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000282076; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR013783; Ig-like_fold.
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:SF32; PENICILLIN-BINDING PROTEIN 2A; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS50853; FN3; 2.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:RKP55344.1}; 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:UP000282076};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 821..915
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 943..1032
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 902..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 112661 MW; 17B23A8647F1AED7 CRC64;
MTNTKTPPSE PIPRGEGFKT AGKIAGFTVL WLILFGVLAG LVGAGAVTGF IASLVHDDPI
RPRSLIEEKI DENAITGFVY FNDGTPIGQL RSEEDRRPVK FEQIPQTIID AVVSIEDKNF
FTHHGVDTNG LLRAVKQQLL NESVQTGGST ITQQVARRVF LSLDQTSSRK AKEIFLSLRL
ERFMSKEEII TAYLNKIPYG NGSNGYQVYG IKAAAKGIFG IESLDKLNIA QAAYLAGVPQ
LPSLYSAFNG KGDFNEKNFN RAVQRQKLVL SRMLDEKKIT QAQYEEALSF DLYKSLAKTS
EKAYNTYPYL MLEVERQAAE ILVLKENPTL TAADLKKKEN ASLIEDARGQ LLRGGYKIKT
TIDKKVYNIM HEIAENPKNF SPDNPVKGVE QIAAVMIDQK TGAILGMLEG RDFHIEQMNF
ATQMTRQPGS AMKPIAAYLP AIDKGLIQPA SILDDSPIIL KNGGGGYHIP KNSNGYYSGL
VTARQALNSS YNIPALKIFL DKLGIKESWD FVRSLGITTL VKEDDGAQTG VIGGLKYGVT
VEELTNAYSA IGNKGVFNDA YLIDEILDPN YKPIYKHEAD PKRIVSEQSA YLMTDMLRTV
VTNGTATKTL QSKFKHFGKI PVVGKTGTTQ NYGDVWFQGY TPDITLGVWS GYEQVIHTLS
EDGKNRAKTV WAQIMDGVID AKPELFPTKS FDMPDGIVSM TVSSVSGKLP TELTKQAGRL
VTDIFNRKFI PTEEDDALVK VKYISYNGVN YLPQADTPED LLRESVMVVR ETPLDTLMEE
LQAKLGQVSA QSRKALSYYL PRDAAQSAPS KIDPRVDDGA VPSAPARVTV ENLNNLARIT
FTPSLQADVA GYRLYRSTNG GPYQKVEASI PAGDEPKFVN YISSSQVYSY YVTAVDVAGN
ESAPSEKISS ESGQGTDPYF PIENPDDGTG SPGDPNGGTN NRNPSVPSGL SAQASEIGVS
LAWNANPGGE GVSKYQVWYS TTEKGKYKLL GTAETTSFEY IAPLSAGWYR VTAVSASGES
SPSVSVEVKT GG
//
