ID A0A1V3P726_9GAMM Unreviewed; 793 AA.
AC A0A1V3P726;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=B0E52_10400 {ECO:0000313|EMBL:OOG42161.1};
OS Rhodanobacter sp. C06.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1945854 {ECO:0000313|EMBL:OOG42161.1, ECO:0000313|Proteomes:UP000189228};
RN [1] {ECO:0000313|EMBL:OOG42161.1, ECO:0000313|Proteomes:UP000189228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C06 {ECO:0000313|EMBL:OOG42161.1,
RC ECO:0000313|Proteomes:UP000189228};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-2017) 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:OOG42161.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MUNP01000049; OOG42161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3P726; -.
DR STRING; 1945854.B0E52_10400; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000189228; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000189228};
KW Transferase {ECO:0000256|PIRNR:PIRNR002799};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..156
FT /note="Bifunctional transglycosylase second"
FT /evidence="ECO:0000259|Pfam:PF14814"
FT DOMAIN 167..338
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 432..669
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 765..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 793 AA; 85648 MW; 732CACDFF44F804C CRC64;
MYVQDSPALL TRTRSFLRAA WPWLRIPFWI ALGLLVGFVL PYTLVLNKRV QERFNDLVFA
VPTRVFARPL PLAAGEPMTS AALQLELTFA GYSDDGHGQV PGSWAKQGAR YTISSRGYAG
PEGGELPKRI EVRLGNGTIA SVRDLATGKP VELAHLDPAR IATVYGAQQV DRRIVRLADL
PPLLVSGLQA VEDRSFKHNI GIDFGGILRA AFANLRAGRT VQGASTLTQQ LVRNLYLSRQ
QTFTRKINEA LMSLLLELHY SKDRILEAYV NEVFLGQQGG QAVHGFAAAA EFYYGRPLRD
LRPQEIAMLV GLVKGPSYYD PRRSPERALA RRNLVLQEFV DTGLLSAAQA KEAQAAPLDV
IKNGQLPHDR FPAFMQLVRQ QITSDFDEDT LRAGNLSIFT TLDPAAQLYT EQAIDTTMKE
LGKRADPLQA AGVVTDAHDG SVLAVVGSKI PGDQGFNRAL DSQRPIGSTI KPFVYLVALT
DPARWNLATA LDDSPISMRM QNGTLWEPHN DDNQSHGMVP MVDALAKSWN LASIRLGLAV
GLPRIRAFLQ SFGLTDVNSG PSLLIGALDL SPLQVAQLYE YIASDGHALP LLAVRGVVDG
NGRTIKRYEV QSGKGEYQEA VRLVTWAMQQ VTTYGTASSL GNSSLASLHV AGKTGTSNDL
RDSWFAGFTG EHLGVFWMGR DDNKPAHLFG ATGALRVWRN LFAKLPTRPL SAAPGDGLQM
AWVNPADGKP TEQQCSGAKQ VPVVTGSLSG DVEGCGFWQS LFGGGSPAAP SSSSAPVNPG
TAPVAIPSLS SGN
//
