ID A0A0M3ATT9_9SPHN Unreviewed; 845 AA.
AC A0A0M3ATT9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN ORFNames=YP76_10585 {ECO:0000313|EMBL:KKW92356.1};
OS Sphingobium chungbukense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=56193 {ECO:0000313|EMBL:KKW92356.1, ECO:0000313|Proteomes:UP000033874};
RN [1] {ECO:0000313|EMBL:KKW92356.1, ECO:0000313|Proteomes:UP000033874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ77 {ECO:0000313|EMBL:KKW92356.1,
RC ECO:0000313|Proteomes:UP000033874};
RA Kim Y.-C., Chae J.-C.;
RT "Genome sequence of aromatic hydrocarbons-degrading Sphingobium
RT chungbukense DJ77.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034000};
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}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004249}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004249}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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:KKW92356.1}.
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DR EMBL; LBIC01000004; KKW92356.1; -; Genomic_DNA.
DR RefSeq; WP_046763563.1; NZ_LBIC01000004.1.
DR AlphaFoldDB; A0A0M3ATT9; -.
DR STRING; 56193.YP76_10585; -.
DR PATRIC; fig|56193.3.peg.2194; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000033874; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; 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; IPR031376; PCB_OB.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF27; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF17092; PCB_OB; 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 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
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 Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..263
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 359..456
FT /note="Penicillin-binding protein OB-like"
FT /evidence="ECO:0000259|Pfam:PF17092"
FT DOMAIN 458..749
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 845 AA; 93277 MW; B5C795274DA066F2 CRC64;
MEEARPENAA SSFSQRLRRG ASDFRQRLQP HWDKRWFRWI AVGLGGLLLA YAAFWLLFAR
GLPDAATLLE YEPPLPTIVR DTDGQPVHSY ARERRVQLQY SDYPPLLIRA YLSAEDKTFF
EHHGVDIPGF FGAVFDYATK IGSGQRARGG STITQQVAKN LLIGDEYSPT RKVKEMILAY
RMEGVLTKQQ ILELYLNQIF LGRNAYGVQA AARAYFDKDV GDLKLHEMAY LAILPKGPAN
YRPESPTGHE RALERRNWAL GEMAKNGWIT KAQRDEAQAQ PLGTVAAHGS SFDARAGGYY
MEEVRRRLIQ LFGEKAEDGP NSVYAGGLWV RSPYDPKMQD LTTTALRNGL LRFDAGKGWS
GPVGKVDMAR GWQRELAASY IDVDYAGWRV AVIVNRDSSA AQIGFSDGST GTLPADAAQL
PYRKSGGPAF AAMKPGDLIV VARNGSSWAL RNVPEVSGGM VVEETHSGRV RAMQGGFDNR
LSSYNRATQA MRQPGSTIKP FVYAAALDNG MTPASIIVDG PLCVYQGAGL GQKCFRNFTG
GSAGPQTMRW GVEQSRNLMT VRAASQTGMD RVVRTIKAMG IGDYQPYLSF ALGAGETTVE
RMVNAYAMLA NQGRQLSPKL MDYVQDRRGK VIWPLRWRAC DGCNMANWDG KPMPRFGFEG
RQVMNPMTAY QVVHIAEGVI QRGTATVLAD LKRPLFGKTG TTNGPTNVWF VGGSPDIVAG
VYIGYDQPRS LGGWAQGGRV AAPIWKAAMT PVLETMPKTP FVAPAGIRMV TIDRRSGKRV
YGVWPTDEPK PAVIWEAFKP ESEPRRSIRK EEVAAQDKAA ARIEATVQRH QRTDSDFLQD
QGGIY
//
