ID A0A170PH09_9CHLR Unreviewed; 1211 AA.
AC A0A170PH09;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 2.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=CFX0092_A2179 {ECO:0000313|EMBL:CUS04057.2};
OS Candidatus Promineifilum breve.
OC Bacteria; Chloroflexota; Ardenticatenia; Candidatus Promineifilales;
OC Candidatus Promineifilaceae; Candidatus Promineifilum.
OX NCBI_TaxID=1806508 {ECO:0000313|EMBL:CUS04057.2, ECO:0000313|Proteomes:UP000215027};
RN [1] {ECO:0000313|EMBL:CUS04057.2, ECO:0000313|Proteomes:UP000215027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cfx-K {ECO:0000313|EMBL:CUS04057.2,
RC ECO:0000313|Proteomes:UP000215027};
RA Oliw E.H.;
RL Submitted (JAN-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; LN890655; CUS04057.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A170PH09; -.
DR KEGG; pbf:CFX0092_A2179; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000215027; Chromosome i.
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; 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:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000215027};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 258..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 320..491
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 584..878
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..244
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1211 AA; 129102 MW; 5E570EC4288C4567 CRC64;
MQDETDRQPD ETPTGGERRS SPLQPYPKPD NPPEEPETIS LLDLMAQESE EQGQITIELP
PEALTVELPP LVPSNPPAVV PPPPAADDDD DQDTPTSTIP PLGQPPAGQS GGSGRTERPL
TRQEFEPEPR PTVEDTEATT VQPRTAFPGA TQIRRPQTTD HRPQATDQRP PTTDHRPADS
EQTTQVRPRP AAGGRPTSPP PTATSRPSSP PPTTAGRPPS PPPPRSPSAA GRPPSAPPPP
IQSHVEQPMT AGRIGRGLLV TLLVLFVGGL LLASTAAIGY SLVAGDLPRP SELRDRASSF
ETARIYDRNG QLLYAPVDPN TGNRTYVPLA RISPYLVQAT IATEDKRFYD NPGFDIIGLG
RAVIMAAREQ EAVAGTSTIT QQLVRATLLD EDERTERSYR RKVREIILAA EISRTYSKEE
ILELYLNEIY YGNLAYGIEA AANTYFNKSA ADLTLAEASL LAGLPQAPAL WDPYTAPDKA
LGRQREVLSL MVANDLITLD DAQAALDEMA GRVYTLQRPE VTIRHPHFTF TVLQQAEELL
GAQSLYRGGL SIRTTLDPDA QRLAEEAVAA NREAINVGGA NNAALVALQP QTGEILAMVG
SADFNDEAIS GQVNMALAPR QAGSTIKPLV YLAAFERGWT PATLLWDVQT EFPDGANPVY
VPKNFDDEFH GPLRIRPALA NSYNIPAVKT LEFVGVCEFI ANVQKVGLTN LQDPGCAEAG
TPRNYGLSLA LGAGEVPPLQ LAGAFGALAN GGRYTAPYAI SRIEDRQGNV LYEAPAPGAA
ATQAMREEHA YLLTNILSDN NARLAEFGQN NTLIIPGYQV AAKTGTSGST ADDVRDGWTI
GYAPQVLTAV WVGNTDNRPI GSGQSGYRLA SPIWNRFMSS YLNGREALAF VRPPAVIDRE
ICADTGIAVG PDSTCGPRVT EVFAGDQPPQ DASQGVTRVA IDLWTGLQAN TSCNDAVYEA
TFGGGVPVNG RPDVLERERV LATNWMQQTP AGQSWAAAQG FSSAAATPPT QACDANTPRP
RAEIVRPRNE ADAPDRAAIE IWGTAMGPNY QGYQVEYGLG ENPGGWGMIQ ERRPEAVQDG
RLAVWDASQI AYSGPVTIRV IVFGPDNPFT PENDPVLKEG RTVFNLQAPT PTPTATATQT
PTATATGTAT PTITATPTAT TTGTATTTPT ATPTASATTP VEPPTAEPPT ETPTSTTEAP
TALPNAVTPY P
//
