ID A0A1G6HAY4_9BACI Unreviewed; 861 AA.
AC A0A1G6HAY4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05421737_103123 {ECO:0000313|EMBL:SDB91294.1};
OS Shouchella lonarensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Shouchella.
OX NCBI_TaxID=1464122 {ECO:0000313|EMBL:SDB91294.1, ECO:0000313|Proteomes:UP000242662};
RN [1] {ECO:0000313|Proteomes:UP000242662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=25nlg {ECO:0000313|Proteomes:UP000242662};
RA Varghese N., Submissions S.;
RL Submitted (SEP-2016) 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};
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DR EMBL; FMYM01000003; SDB91294.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6HAY4; -.
DR STRING; 1464122.SAMN05421737_103123; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000242662; 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; 1.
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 NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF29; PENICILLIN-BINDING PROTEIN 1A/1B; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 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:UP000242662};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 697..772
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|SMART:SM00060"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..802
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..825
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..861
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 95052 MW; A2FD5EE8FA466B7A CRC64;
MSDRFKSRQE RKQAQRKKGA SSKKPRSLFK KILLTMAILF GIGVVGGGTT IAIMIATAPD
LDPEKLTLIQ SMQIYDMNDE LVSTLDASEF RVSANIQDMP DHLKNAFIAV EDQRFYDHFG
IDLKRLGGAI WANITGGFGA EGASTITQQL VKNLFLTNEK ALTRKVQEQY LAIQLERKYS
KEEILEMYLN QINLGPSAGY GVQIAAETYF NKSLDELSVA DAAVLAAIPR RPTFYDPHRN
PENAEGRRNT VLNLMEEQGF ITKEEADEAR NTPIADQMDY TTKERYAYAT FYDEVLDELQ
DNEELASNNL LNSGLKVYTT LDPKAQESVD RVLKSGEYQG LVFPQDNEDF KVGVTLVDTK
SGAVRAFGND IKENNQRDWN HATDPKQQGS AMKPLLAYAP GIEMNKWSTA KVLVDEKHNY
TDGTPISNAN NSYLGAMTMR EALVRSRNIP AVKAMQEVSK DEAYAFLDPM IKIPETTKDK
DGKVTHHRVE AGVLGGTQVS TKQMAGAYAA FGNGGTFTEP YIIRKVVFPD GREMNMEPES
EKVMEDYTAY MVTDMLKDVI NNPIGTGKAA KVAGIPVAGK TGTTNFNDKV RAHYNITDPN
AYPASTFSGY STNYTASVWM GFSKNGENNY LTDAHKTTAQ SIFKHIMTEV HKGVDTPDFV
KPDSVVVRNV KTPSDQISRE LFVRGTEPEE IPENTGISDP SKLTADYDKD TNTLTFSWDY
PEDEREEVNF EASIDKGSLQ VNQNEMKAVF TNVTPGETYT FTVKAVSANE ESKAVILKVT
PGAANDEDEE ENEEEPPEPT PPGDDDNGDS PPPSNGRPPE EEAPPSNENP GDGDTTSPPN
DGDGDGGDTE TPVEPDPPDE E
//