ID A0A1R4GUV4_9GAMM Unreviewed; 851 AA.
AC A0A1R4GUV4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 Name=mrcB {ECO:0000313|EMBL:SJM71612.1};
GN ORFNames=A1232T_01278 {ECO:0000313|EMBL:SJM71612.1};
OS Psychrobacter piechaudii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1945521 {ECO:0000313|EMBL:SJM71612.1, ECO:0000313|Proteomes:UP000188357};
RN [1] {ECO:0000313|EMBL:SJM71612.1, ECO:0000313|Proteomes:UP000188357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Psychrobacter_piechaudii {ECO:0000313|EMBL:SJM71612.1};
RA Peterson S.W.;
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}.
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DR EMBL; FUGE01000130; SJM71612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4GUV4; -.
DR STRING; 1945521.A1232T_01278; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000188357; 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; TIGR02074; PBP_1a_fam; 1.
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:UP000188357};
KW Transferase {ECO:0000256|PIRNR:PIRNR002799};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..169
FT /note="Bifunctional transglycosylase second"
FT /evidence="ECO:0000259|Pfam:PF14814"
FT DOMAIN 182..352
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 451..708
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 851 AA; 93784 MW; 3D7750FDF1595A1F CRC64;
MHHKPSLAKS PISKSSASSL NTFTGKTPNP EQQRGSVLGF LLLIIIIVGM VILAMYLIKQ
DRVITAKFEG KRWNIPAKVY SQPLELYQGA TLTTKNLDSW LEMLNYKSSS NYDRTGTYNK
SSGQYVIHTR GFQYSASDVD PEQVIKIKIQ DSKITSIQST QPSDTGIVRI EPVTIGGIYP
DNNEDRIVLP ISEIPQPLID ALISTEDRGF YQHKGVSLKG IGRAFYNNLQ GGSMQGGSTI
TQQLVKNFYL SSDRTLKRKA NEAVMALLLE MHYSKDEILQ TYLNEINLGQ NGNRSINGFG
LAAQFYFNQP LKELRIDQQA LLVGLAKGTS YYNPRRNPER ALDRRNTVLA NMLATGKIDQ
ETYEEAIAKP LDVVEKPSVG KSRFPDFLDI VKRELQSNYH PEDLKNEGLR VFSTLDPIAQ
FAADNAVQKQ LSVLRKKSSK TKPLQAALLS ANPASGELVA AIGSGSEFTG FNRAVDAKRQ
VGSLLKPFIY MTALESGKYN LASSVNDSPV TLNLSDGSSW TPKNYDGVDH GYVPLTTALA
KSYNQAAVNT GVEFGVGTLV NQMHRLGINE KIPTYPSLFL GSVELSPMDM LGMYQVVAAG
GFRTPIISIR TVVDDRGSIL QRSGFDTKRS VPPDVNYLTN YALQEVVRNG TASSLKSLGS
DLNLAGKTGT TNDYRDAWFA GYSGNYVSVV WVGRDDNKPI GLSGGSGALP LWKDFMGRLR
LTPVELVQPD SVEWLWLENG TGKLSHESCP GARYLPVLSR SLPEDASDCA LELYQQEQSR
QQMRWLNDQR KALLNRSREL DSVQEGMPSG ASNGENNEGG MGSQNDEGGA SNNNNSENSG
DTWYDKALEW F
//
