ID N4W6E2_9BACI Unreviewed; 986 AA.
AC N4W6E2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=J416_14148 {ECO:0000313|EMBL:ENH95783.1};
OS Gracilibacillus halophilus YIM-C55.5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=1308866 {ECO:0000313|EMBL:ENH95783.1, ECO:0000313|Proteomes:UP000012283};
RN [1] {ECO:0000313|EMBL:ENH95783.1, ECO:0000313|Proteomes:UP000012283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM-C55.5 {ECO:0000313|EMBL:ENH95783.1,
RC ECO:0000313|Proteomes:UP000012283};
RA Sugumar T., Polireddy D.R., Antony A., Madhava Y.R., Sivakumar N.;
RT "Draft genome sequence of Gracibacillus halophilus YIM-C55.5, a moderately
RT halophilic and thermophilic organism from the Xiaochaidamu salt lake.";
RL Submitted (MAR-2013) 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:ENH95783.1}.
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DR EMBL; APML01000074; ENH95783.1; -; Genomic_DNA.
DR RefSeq; WP_003473636.1; NZ_APML01000074.1.
DR AlphaFoldDB; N4W6E2; -.
DR STRING; 1308866.J416_14148; -.
DR PATRIC; fig|1308866.3.peg.2851; -.
DR eggNOG; COG0744; Bacteria.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000012283; 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 Gene3D; 3.90.1310.40; -; 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; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
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; 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:UP000012283};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..282
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 430..680
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 787..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..953
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 110354 MW; 7A67B6594178BE45 CRC64;
MKLKELFTKY WDSIKDVWDK YKIQKKARIG YHIVWNAFLF FLVLMVVGIF FVGGLGAGYF
ASLVDEQEMY SEEEMTEAIY TYEETSELYF NNNEFLAEVS SDLLREEVTI DQVSQTAKDA
VIATEDENFY SHEGVVPKAI FRAVVQQVTN SATQTGGSTL TQQLVKNQIL TNEVSFERKA
KEMLLSMRLE QFIDKENILE AYLNIVPYGR NASGQNIAGI QTAAKGIFGV NANELNLPQS
AYIAGLPQSP SIYTPFKNGG GVKSDEELEP GLNRMESVLE RMYENEFISQ EEYQNALNYD
IVADFKEPEP SVLEKYPWLT QTIQERAIDV LTTILAKEDG YTEDELESSS VLKEEYEIRA
QRALESNGLK VHSTIDEEMY DVFQEIAKEY NNYGPDKVAR NARGEVITVE NPETGEEERL
GKQPVQVGSV LIENQTGKIL SFVGGRDFTE SQKNHALDVR RPNGSTMKPL VTYAPAMEYG
VIQPGSVIAD VYDPSMPGYP SYDPPRNYTG SYYGLVSARE ALYRSHNVSA LQIYRQIRDR
NPAAQFLENM GFDHLSQDAG DYMNMSLTLG SPHNGVTVEE NVNAYATFGN MGDFVEGYMI
ESIETKDGEV LYEHESKAEE VFSEQTSYLM VDMMRDVLSR GTGTAAYANL GNRSVDWAGK
TGTSNDYRDT WFVATNPNVT LGSWMGYDYN QSLSSGYSSR NNVFWAELVN AATEIRPDLM
APSSSFDQPN GIVSRSYCKT SGKLPSDLCS ELGLVGTDIY NSNHVPTEED NSLIDAEYAL
IDGEAVPSGE DTPEEFTDDD GVSFNPDWLE EKGYDQLPNI EQLKPSDSGA WGDIQFPGET
AEINGDSDSP APPTSLQFDN NQLNWNTSNS NDVVGYRIYR ANNPDGNNFQ RVGHTSETNF
TVPNGPALYH VKAVDYFGQE STSSESIIFG EFSEPEDENE EEEEEDQKEN NQQDNDENDD
SNNSNGEDET NQNSEDSENS NNSNNS
//
