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Database: UniProt
Entry: A0A1G6HAY4_9BACI
LinkDB: A0A1G6HAY4_9BACI
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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
//
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