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Database: UniProt
Entry: A0A249L5L0_9ACTN
LinkDB: A0A249L5L0_9ACTN
Original site: A0A249L5L0_9ACTN 
ID   A0A249L5L0_9ACTN        Unreviewed;       651 AA.
AC   A0A249L5L0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, 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=B1sIIB91_05885 {ECO:0000313|EMBL:ASY24390.1};
OS   Candidatus Nanopelagicus abundans.
OC   Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC   Candidatus Nanopelagicaceae; Nanopelagicus.
OX   NCBI_TaxID=1884916 {ECO:0000313|EMBL:ASY24390.1, ECO:0000313|Proteomes:UP000217210};
RN   [1] {ECO:0000313|EMBL:ASY24390.1, ECO:0000313|Proteomes:UP000217210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS-IIB-91 {ECO:0000313|EMBL:ASY24390.1};
RA   Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT   "High microdiversification within the ubiquitous acI lineage of
RT   Actinobacteria.";
RL   Submitted (JUL-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; CP016779; ASY24390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A249L5L0; -.
DR   KEGG; nab:B1sIIB91_05885; -.
DR   OrthoDB; 7911552at2; -.
DR   Proteomes; UP000217210; Chromosome.
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   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF34; PENICILLIN-BINDING PROTEIN 1A; 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:UP000217210};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          55..231
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          323..570
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   651 AA;  69958 MW;  016D70E1233EDE73 CRC64;
     MNNLLAKLPR LGVLITGFSF VAGVFLFGFA YFTVSIPDPN AYVNSQSTII QYADGSEIGR
     IGSENRTVVT LAQIPVQVRN AVMAAEDRGF YSNRAISPTA IIRAVWNNVR GGSLQGGSTI
     TQQYAKTAFL TPERSITRKV KELVIAIKLE NQFTKDQIFE NYLNTIYFGR GSYGVQTASQ
     VYFGTTVDKL TTAQSAVLAS ILRSPGLYDP GFKKENLPRL EKRFTYVLDG MVAQGWLEKE
     KAEKIKFPVI NPRVTSGALA GPKGYVISWV ERELNALGFS DEQLMVGGYI IKTTLVKEAQ
     EAAVFAVSKE APVKVPENLH IGLVAIKPGT GEILAMYGGQ DYLKYQFNAA TQGITSGGSS
     FKAFSLVAAL EQGIPLSSIW NGDSPKVYDD GIGRPYPVNN YGGESWGNLD LLTATEKSVN
     TIYVPLGMKA GLEKVVDVAR RAGIPESVEM VASPSVSLGA ASPHVIDLAN AYATFAAQGV
     YAKPFIINEV QGPNKGILYQ GRIQAQEVFR KDVMADLTYA FSKVTTSGTA AVVGARVGRP
     TAGKTGTSND NASAWFNGYT PEVAASVAFY RDDATQSLNG IGGLTSVTGG SFPARIWAEF
     VKKYLAKSLI QEFPAPAFIG GTEPVNFINA VPEMDPALIP PSPSPSPKKK K
//
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