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Database: UniProt
Entry: A0A1I2V7K3_9BACT
LinkDB: A0A1I2V7K3_9BACT
Original site: A0A1I2V7K3_9BACT 
ID   A0A1I2V7K3_9BACT        Unreviewed;       780 AA.
AC   A0A1I2V7K3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=SAMN05421739_10478 {ECO:0000313|EMBL:SFG85348.1};
OS   Pontibacter chinhatensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Pontibacter.
OX   NCBI_TaxID=1436961 {ECO:0000313|EMBL:SFG85348.1, ECO:0000313|Proteomes:UP000198724};
RN   [1] {ECO:0000313|EMBL:SFG85348.1, ECO:0000313|Proteomes:UP000198724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LP51 {ECO:0000313|EMBL:SFG85348.1,
RC   ECO:0000313|Proteomes:UP000198724};
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};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; FOOT01000004; SFG85348.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2V7K3; -.
DR   STRING; 1436961.SAMN05421739_10478; -.
DR   Proteomes; UP000198724; 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: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; 2.
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   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   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        21..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..265
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          442..687
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   780 AA;  88712 MW;  471B0FE42F4908F2 CRC64;
     MLKMPKEQEK VQEPKKTSSS IASKVISFTW KIFFLGLFVI LGYLFSVEYN VLYLFGSSPS
     LDRLENPRSD QASELYTADG KLIGKYFREN RSPVTYQELS PELVQALLAT EDIRFYEHAG
     IDPEAIVSAV YGSFQGEARG ASTITQQLAK NLYKTRTDDS KGVLGHIPGL SIVISKTKEW
     LTAIKLEQRY TKEEILTMYL NTVDFGSNSF GIKVASKTFF NTTPEKLKTE QAAVLVGLLK
     APTYYSPRFN PENATRRRNV VMGQMVKYGY LDKAKADSLS QLPLVLDYSV ENHYDGPATY
     FRGAVADYLQ EWCKENGYDL YRDGLKIYTT IDSRMQAHAE AAMEEQMRKL QRRFYSHWEG
     KKPWVDEKNR EIPGFIEETI KRTAYYRRLK QKYGDDMEAI NKELNRPREM KVFTWDNDSL
     EKTVTMSPLD SLAYYKHFLH GGMMTMDPFT GHIKAWVGGI NYKYFKYDHV KQARRQPGST
     FKPFVYVAAI DNGYSPCDKI VDQRITINYV EKGEKKSWSP TNADWQYTGA PMTLRRGMGK
     SVNSVTAQLT ELIGWETVVK YAHKLGIKSP LQAVPSIGLG PSDVSVFEMV GAYSTFPNYG
     FHTEPMFITR IEDHNGNLLH QFTPIQKKVL SEETAFLMMH MLKGGIEEPG GTSQALWEYD
     LWKGNEIGGK TGTSSNHSDG WFMGVTKDLV TGVWVGGEDR SIHFRTSQLG EGSKTALPIY
     GLYMERIYQD EELGYTMGRF PKPTVKISKK YNCTTVLPKA QPDSTLLDPM LELLNIGDIL
//
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