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Database: UniProt
Entry: H0TDA6_9BRAD
LinkDB: H0TDA6_9BRAD
Original site: H0TDA6_9BRAD 
ID   H0TDA6_9BRAD            Unreviewed;       828 AA.
AC   H0TDA6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
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=BRAS3843_1070044 {ECO:0000313|EMBL:CCE04444.1};
OS   Bradyrhizobium sp. STM 3843.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=551947 {ECO:0000313|EMBL:CCE04444.1, ECO:0000313|Proteomes:UP000002686};
RN   [1] {ECO:0000313|Proteomes:UP000002686}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=STM3843 {ECO:0000313|Proteomes:UP000002686};
RX   PubMed=24704842; DOI=10.3390/genes3010035;
RA   Mornico D., Miche L., Bena G., Nouwen N., Vermeglio A., Vallenet D.,
RA   Smith A.A., Giraud E., Medigue C., Moulin L.;
RT   "Comparative genomics of aeschynomene symbionts: insights into the
RT   ecological lifestyle of nod-independent photosynthetic bradyrhizobia.";
RL   Genes (Basel) 3:35-61(2011).
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:CCE04444.1}.
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DR   EMBL; CAFK01000010; CCE04444.1; -; Genomic_DNA.
DR   RefSeq; WP_008966969.1; NZ_CAFK01000010.1.
DR   AlphaFoldDB; H0TDA6; -.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002686; 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; 2.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR031376; PCB_OB.
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: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   ECO:0000313|EMBL:CCE04444.1}; 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:UP000002686};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..236
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          325..446
FT                   /note="Penicillin-binding protein OB-like"
FT                   /evidence="ECO:0000259|Pfam:PF17092"
FT   DOMAIN          448..743
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   828 AA;  90960 MW;  FB5581523D69D05A CRC64;
     MRLLMRFFSF FFAAGTVVFL IGAAAVAGLF WHFSKDLPDY SQLQNYEPAV MTRVHAADGS
     LVGEYARERR LYLPIQAVPK LVINAFLAAE DKNFYEHGGI DFSGMARAAL AYAQHFGSDR
     RPQGASTITQ QVAKNFLLTN EVSFTRKIKE ALVAMRIERA YSKDKILELY LNEIYLGSGA
     YGVAAAALVY FDKSVNELTV AEASYLAALP KMPGSLHPIR NHDRAIERRN YVVDRLFENS
     WINKADADAA RREPITISTH AGSAHTFAGE FFAEETRRDL FDRYGEKKLY EGGLSVHTTL
     DPKIQVMARK TMVAGLVRYD EEQGYRGPVS KLDISGDWGV KLAEIKSLSD ISPWRLAVVL
     ETSGQSARIG FQPGRELGAL SKERQTGLIS LEGVKWARAA SGPGRGRTPS SVAQVLQPGD
     VIYVDPLYKE GRPVEGQYRL EQLPEVSGAM VVMEPNTGRV VAMVGGFSFD QSQFNRATQA
     YRQPGSTFKP IVYSAALDNG YTPSSMMVDA PIEVDQGEGG DVWRPDDFSN GKYLGPTTLR
     NALRLSLNTV TVRLAQDIGM PLISEYAKRF GIYDEVPNYL SYSLGTGETT VMRMVTAYSM
     IANGGRRVKP TLIDRIQDRY GHTIFRHDAR ECRGCEAPEG WHNQAEPQLV DRREQVLDTM
     TTYQITELME GVVQGGTAIA LKEVGKPIAG KTGTTNEAKD VWFVGFSPDL VIGLYVGYDK
     PRSLGRTAQA ARITAPIARD FMKLALIDKP ATPFKIPAGI KLVRVDARTG MRAVPGQAGA
     ILEPFKPGTA PPDSFSTMSE ADPDRALVPQ GTALDTGAVM RPGTGGLY
//
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