ID A0A2I9DFM8_9FLAO Unreviewed; 796 AA.
AC A0A2I9DFM8;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpF {ECO:0000313|EMBL:GBF18128.1};
GN ORFNames=C21_00285 {ECO:0000313|EMBL:GBF18128.1};
OS Arenibacter sp. NBRC 103722.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Arenibacter.
OX NCBI_TaxID=1113929 {ECO:0000313|EMBL:GBF18128.1, ECO:0000313|Proteomes:UP000095208};
RN [1] {ECO:0000313|EMBL:GBF18128.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C-21 {ECO:0000313|EMBL:GBF18128.1};
RA Ito K., Nakajima N., Yamamura S., Tomita M., Suzuki H., Amachi S.;
RT "Draft Genome Sequence of Arenibacter sp. Strain C-21, an Iodine-
RT Accumulating Bacterium Isolated from Surface Marine Sediment.";
RL Genome Announc. 4:e01155-16(2016).
RN [2] {ECO:0000313|EMBL:GBF18128.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C-21 {ECO:0000313|EMBL:GBF18128.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-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 -!- 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:GBF18128.1}.
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DR EMBL; BDGL02000001; GBF18128.1; -; Genomic_DNA.
DR RefSeq; WP_051892275.1; NZ_BDGL02000001.1.
DR AlphaFoldDB; A0A2I9DFM8; -.
DR Proteomes; UP000095208; Unassembled WGS sequence.
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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000095208}.
FT DOMAIN 78..238
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 316..592
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 704..789
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 796 AA; 89802 MW; 52BB67E772069A3A CRC64;
MNLGTDKGPD KAATTLQRLK GLIQRHPKKL LILILLLIAY YFCLPKQLFR TPHATVVESR
SGKLLGALIA EDGQWRFPVV DSVPYKFETC ILNFEDAHFY WHPGFNPISI GKAFLANILA
GKTVRGGSTL TQQVIRLSRN HKKRTYWEKV RELVLATRLE LGYSKKYILK LYASHAPFGG
NVVGLEAAAW RYFGMQPNQL SWAEAATLAV LPNAPSLIYP GKNHSKLLYK RNRLLHKLLD
NNYIDSTTYR LSLLEELPKK PFQLPDTAPH LVQYLAKKYK GKRISTHVDE NLQGSINNII
NKHYKSLKQN QVYNAAVLLM DVKTREVLSY VGNTPTDNEH EKDVDMVQAN RSTGSVLKPL
LYTAMMNAGE LLPGMLIPDV PTQIAGYTPE NFNESYSGAV EADKALAKSL NIPAVRLLRS
YGLQKFRDQL DFFNLRGLDK SADHYGLTLI LGGAESNLWD LCKTYASLAS TVNHFNATSS
EYYTKEFVEP IPTSETKVDF GAKSTEVTIF DAASIYLTFE AMKKVNRPEG SESWEFFDSS
RQIAWKTGTS FGNKDAWAIG ITKDYVVGIW AGNADGEGRP NVTGLSSAAP ILFDVFDLLP
RSTWFQKPED EFTEIKVCSE SGYLATDICP KTVISIPRKQ NFVQACAYHQ WVHLNVQKQF
RVNSSCADLS EMFSESWFVL PPLMEYYYKK GHPSYKTLPP FLENCRETNT AAMEFIYPRN
GSRITLARNF EGKKNELVVK LAHVKPETPV YWYLDEKFIG QTTDYHEIGL MPIPGEHGIM
AVDALGNEVV IIITIE
//
