ID A0A432W471_9GAMM Unreviewed; 757 AA.
AC A0A432W471;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:RUO24288.1};
GN ORFNames=CWE09_10440 {ECO:0000313|EMBL:RUO24288.1};
OS Aliidiomarina minuta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Aliidiomarina.
OX NCBI_TaxID=880057 {ECO:0000313|EMBL:RUO24288.1, ECO:0000313|Proteomes:UP000288293};
RN [1] {ECO:0000313|EMBL:RUO24288.1, ECO:0000313|Proteomes:UP000288293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MLST1 {ECO:0000313|EMBL:RUO24288.1,
RC ECO:0000313|Proteomes:UP000288293};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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:RUO24288.1}.
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DR EMBL; PIPL01000002; RUO24288.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432W471; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000288293; 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:UP000288293};
KW Transferase {ECO:0000256|PIRNR:PIRNR002799};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..140
FT /note="Bifunctional transglycosylase second"
FT /evidence="ECO:0000259|Pfam:PF14814"
FT DOMAIN 145..323
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 412..666
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 757 AA; 85186 MW; 809C75078BD020CD CRC64;
MNKWLSSAGW LLLKLSLTGV TILFFYSVYL DSVVTERFEE NRYQAPALLY SRALQISDDK
PLQQGQVLRE LQALNYRHTR YAREPGEFNL RDNMILLHRR AFDFADGFEP SQRLRLRFED
EELAEILAWP TQQPLSVARL EPQLIGRFAA DSGEDRLLVN LEQVPQLMQD TLLLVEDRDF
YQHRGVKPSA ILRAASANLA AGRTVQGGST LTQQLIKNMY LTHDQNLRRK ANEAIMALIL
DYRFSKNEIL EAYFNEVYFG QDRGHAIHGV GLASQYFFGK SVEDLTPAEI ALLVGMVKGP
SLYDPRRRPQ RASARRDLVL RLMYENDLIN QPQYLAAIEA PLVGRESTRL VVRDRPDYVD
LVQRELRQLV PGKEWQQTGL RVFTHYDPYL QEYAEEALQR GVVSLQVADI EGAVVVADHQ
QGVVRALAGS IHPSQAGFNR ALTARRPVGS LIKPFTYALA LEQPERYELN TLLDDSAIVV
TDERDREWQP GNFDGEFRGD VTLYESLVDS RNLPAIRVGL DLGVEKVRER LYNSGLDEPT
HAYPSLLLGA VDMSPLAVTQ LYSVLANQGG QQRLTSIQTV TTHWGHPLYR AQPMTQQVYT
EEASYLTNYA LQGVVREGTG QALGNTLGQS GIAGKTGSTN NLRDSWFVSY DSRHVVTVWL
GRDDNQSVGL SGSRGALPVA AEYWQQAGVE NMLMARPAGL IQGAFNKTTG AAVDLNCEGA
LLLPVRHYEP GRDIDCEGEI KESPEEDEKS WFKRIFG
//
