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Database: UniProt
Entry: V7DAC8_9PSED
LinkDB: V7DAC8_9PSED
Original site: V7DAC8_9PSED 
ID   V7DAC8_9PSED            Unreviewed;       773 AA.
AC   V7DAC8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Penicillin-binding protein 1B {ECO:0000256|ARBA:ARBA00018637, ECO:0000256|PIRNR:PIRNR002799};
DE            Short=PBP-1b {ECO:0000256|PIRNR:PIRNR002799};
DE            Short=PBP1b {ECO:0000256|PIRNR:PIRNR002799};
DE   AltName: Full=Murein polymerase {ECO:0000256|ARBA:ARBA00032454, ECO:0000256|PIRNR:PIRNR002799};
GN   ORFNames=O164_13105 {ECO:0000313|EMBL:ESW39254.1};
OS   Pseudomonas taiwanensis SJ9.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1388762 {ECO:0000313|EMBL:ESW39254.1, ECO:0000313|Proteomes:UP000018511};
RN   [1] {ECO:0000313|EMBL:ESW39254.1, ECO:0000313|Proteomes:UP000018511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJ9 {ECO:0000313|EMBL:ESW39254.1,
RC   ECO:0000313|Proteomes:UP000018511};
RA   Hong S.-J., Shin J.-H.;
RT   "Whole Genome Shotgun Sequence of Pseudomonas taiwanensis SJ9.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan
CC       from the lipid intermediates. The enzyme has a penicillin-insensitive
CC       transglycosylase N-terminal domain (formation of linear glycan strands)
CC       and a penicillin-sensitive transpeptidase C-terminal domain (cross-
CC       linking of the peptide subunits). {ECO:0000256|ARBA:ARBA00002624,
CC       ECO:0000256|PIRNR:PIRNR002799}.
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, ECO:0000256|PIRNR:PIRNR002799}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090, ECO:0000256|PIRNR:PIRNR002799}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739,
CC       ECO:0000256|PIRNR:PIRNR002799}.
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:ESW39254.1}.
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DR   EMBL; AXUP01000164; ESW39254.1; -; Genomic_DNA.
DR   RefSeq; WP_023661650.1; NZ_AXUP01000164.1.
DR   AlphaFoldDB; V7DAC8; -.
DR   PATRIC; fig|1388762.3.peg.2621; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000018511; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:UniProtKB-UniRule.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
DR   GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.30.2060.10; Penicillin-binding protein 1b domain; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR011813; PBP_1b.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   InterPro; IPR028166; UB2H.
DR   NCBIfam; TIGR02071; PBP_1b; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   Pfam; PF14814; UB2H; 1.
DR   PIRSF; PIRSF002799; PBP_1b; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Cell shape {ECO:0000256|PIRNR:PIRNR002799};
KW   Cell wall biogenesis/degradation {ECO:0000256|PIRNR:PIRNR002799};
KW   Glycosyltransferase {ECO:0000256|PIRNR:PIRNR002799};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Peptidoglycan synthesis {ECO:0000256|PIRNR:PIRNR002799};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Transferase {ECO:0000256|PIRNR:PIRNR002799};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          69..152
FT                   /note="Bifunctional transglycosylase second"
FT                   /evidence="ECO:0000259|Pfam:PF14814"
FT   DOMAIN          166..333
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          429..659
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   ACT_SITE        188
FT                   /note="Proton donor; for transglycosylase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002799-1"
FT   ACT_SITE        466
FT                   /note="Acyl-ester intermediate; for transpeptidase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002799-1"
SQ   SEQUENCE   773 AA;  85192 MW;  B9944EA39E63D15C CRC64;
     MTRTRNPRTP QKRPTGRSRA WLGWALKLSL VGLVIVAGFA VYLDAVVQEK FSGKRWTIPA
     KVYARPLELF TGQKLSKNDF LTELDALGYR RESAANGPGA AAVNGNTVEL NTRGFQFYEG
     MEPAQFVRVR FSGDYVAGLS GANGKTLDVV RLEPLMIGGI YPKNLEDRIL IKIDQVPPYL
     LETLVATEDR DFYSHFGVSP KSIARAMWVN TSAGSMRQGG STLTQQLVKN FYLTSERSLS
     RKLTEAMMAV LLELHYDKRE ILEAYLNEVF VGQDGQRAVH GFGLASQFFF SQPLSELKLH
     QIALLVGMVK GPSYYNPRRY PDRALARRNL VLDLVAEQGV ASQAEVDAAK KMPLGVTKRG
     SLADSSFPAF LDLVKRQLRQ DYRDEDLTEE GLRIFTSFDP ILQMKAETSM SETFKRLAGR
     KGADEVESAM VVTNPETGEV QALIGSRQAG FAGFNRAIDA VRPIGSLVKP AVYLTALEQP
     TKYTLTSWVQ DEPFSVKGAD GQVWRPQNYD RRPHGTIYLY QGLANSYNLS TAKIGLEVGV
     PNVIKTIGRL GVNVDWPAFP AMLLGAGGMS PMQVATMYQT IANGGFNTPM RGIRSVLTAE
     GEPLKRYPFQ IQQTFDPGAI YLVQNAMQRV MREGTGRSVY NTLPRNLTLA GKTGTSNDSR
     DSWFSGFSQD LLAVVWMGRD DNGKTPFTGA TGALQVWTSF MKKADPLPLD MPQPDNVVQA
     WIDPYSGHGS DGSCPGAVQM PYIRGSEPPA GATCGGEQDP VESVMDWVKG WMN
//
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