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Database: UniProt
Entry: A0A398CKC4_9BACL
LinkDB: A0A398CKC4_9BACL
Original site: A0A398CKC4_9BACL 
ID   A0A398CKC4_9BACL        Unreviewed;       657 AA.
AC   A0A398CKC4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=D3H35_21800 {ECO:0000313|EMBL:RIE01649.1};
OS   Cohnella faecalis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=2315694 {ECO:0000313|EMBL:RIE01649.1, ECO:0000313|Proteomes:UP000266340};
RN   [1] {ECO:0000313|EMBL:RIE01649.1, ECO:0000313|Proteomes:UP000266340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2E09-144 {ECO:0000313|EMBL:RIE01649.1,
RC   ECO:0000313|Proteomes:UP000266340};
RA   Zhu H.;
RT   "Cohnella cavernae sp. nov., isolated from a karst cave.";
RL   Submitted (SEP-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   -!- 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:RIE01649.1}.
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DR   EMBL; QXJM01000040; RIE01649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A398CKC4; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000266340; Unassembled WGS sequence.
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; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
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   NCBIfam; TIGR02074; PBP_1a_fam; 1.
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   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266340}.
FT   DOMAIN          38..213
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          302..572
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   657 AA;  71656 MW;  753FD466DA9729EB CRC64;
     MTLFGLLTAA GGGYVLLRYG ALPAGSVPQP TQLLGADGTV IAQLEGGVNR RSVRLADISP
     WLIKATLAVE DRRFYEHRGV DVRGLARAAW TDVRHLSKRQ GASTLTQQLA RNLYLSHERT
     WKRKLKEAWY AARLEQTYTK DEILELYLNQ IYYGHGAYGA EAASRLYFGK SAKELTPAES
     ALLAGIPKGP SYYSPHRHPK ESRQRRQTVL QVMKDTGVIS SATADEASHT AVSVRPLPEE
     PEGTAPYFAD YVLKIAESKL GIDERLLHDG GLVIRTTLDA DMQRKAEEAI RDGLPPKSEL
     QGALIAIDPR NGYIKAMVGG RSYRGNQYNR VFASTRQPGS SFKPIVYAAA LERRIVTPAT
     RFRSEPTIFY YDNDRKIYQP SNYADRYFRT EIGMRQAIAA SDNIFAVNTI MQTGAESVIA
     MARRLGIGSP LKAVPSLALG TFPISPFEMA SAFSAFANGG FKYTPLAVLS IRDSKGNTLY
     EAHPRGEQVI SPALAFVTTQ LLESVFQKGG TAYRVSRLLA RPVAGKTGTT DSDAWTVGYT
     PELATAVWLG YDKGRAITSG EAHRAAPIFA NFTESALSGS ASPGLFTMPE GVVTALIDPV
     TGLLATDGCP NPVLETFLSG TEPSASCYVH GSAKEKTGGT ASQKSGAWWK KLRHWWN
//
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