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Database: UniProt
Entry: A0A1H7LC45_9SPHI
LinkDB: A0A1H7LC45_9SPHI
Original site: A0A1H7LC45_9SPHI 
ID   A0A1H7LC45_9SPHI        Unreviewed;       797 AA.
AC   A0A1H7LC45;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SAMN05421740_103115 {ECO:0000313|EMBL:SEK96448.1};
OS   Parapedobacter koreensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Parapedobacter.
OX   NCBI_TaxID=332977 {ECO:0000313|EMBL:SEK96448.1, ECO:0000313|Proteomes:UP000198916};
RN   [1] {ECO:0000313|EMBL:SEK96448.1, ECO:0000313|Proteomes:UP000198916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Jip14 {ECO:0000313|EMBL:SEK96448.1,
RC   ECO:0000313|Proteomes:UP000198916};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNZR01000003; SEK96448.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7LC45; -.
DR   STRING; 332977.SAMN05421740_103115; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000198916; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004180; F:carboxypeptidase activity; 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:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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; IPR011815; PBP_1c.
DR   InterPro; IPR009647; PBP_C.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   NCBIfam; TIGR02073; PBP_1c; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR   Pfam; PF06832; BiPBP_C; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        18..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          70..228
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          311..589
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          708..792
FT                   /note="Penicillin-binding C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06832"
SQ   SEQUENCE   797 AA;  88629 MW;  C4986ACB9642AC8F CRC64;
     MDIRIKDFIA FCKSPKGIFI LAFASTLSLV FYFALPKPLF RSPTSFVIED EAGRLLGASI
     ALDGQWRFPA TDAVPEKFAK CIVAFEDRRF YIHPGVDPVA LVRAIWQNIR GRRVVSGGST
     ISMQVIRMSQ NKPRTIWQKC MEAVLAFRLE AGYNKATILQ LYSAHAPFGS NVVGLDAASW
     RYFGRAPEQL SWAEAATLAV LPNAPSLIHP GRNRKRLLAK RNMLLDKLAV QGTLDRSAAE
     LAKLEPLPDE PLPLPRLAPH LLERFKKEYG RLGTGVTRLK TSINANLQQR VADIIDRHHR
     GLSANGIFNA AALVLEVESG KTMAYVGNVH TPQNAEAESH VDMITALRSP GSTLKPLLYA
     AMLTDGLILP HTLIPDIPTQ IGGYTPQNYD LGYDGALPAS RALSRSLNIP AVKMLQHYKY
     QRFQPFLRQA GVRTLDRPAD FYGLSMILGG CEVTMWQLAG TYASMARTLN HYRRYHAGYN
     STDYRPPHYS RNVGTLPENS VERTSIIDHA SLYFTFQAMN EVMRPGEEAL WEQFASSKKI
     AWKTGTSFGF RDGWAIGLTP THVVCVWVGN ADGEGRPGLT GIETAAPILF EIFDLLPARA
     WFEAPLDRMV QTAVCRESGH LAGPDCPHPD TVYIPVPGHR SSVCPYHQLI HTNSKGTLQV
     TADCAAAGDI VAAQWFVLPP AMEFYYKPRH ATYRELPPFG NGCAIGTDGQ PMEMIYPKNN
     AKIYIPLEID GRRGQVIFNA AHRRKGSRIY WHLDETFVGE TETFHQLALD VPAGLHRITL
     VDSDGARISQ QFEILKK
//
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