ID   C4K4T9_HAMD5            Unreviewed;       793 AA.
AC   C4K4T9;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
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:ACQ67582.1};
GN   OrderedLocusNames=HDEF_0862 {ECO:0000313|EMBL:ACQ67582.1};
OS   Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Hamiltonella.
OX   NCBI_TaxID=572265 {ECO:0000313|EMBL:ACQ67582.1, ECO:0000313|Proteomes:UP000002334};
RN   [1] {ECO:0000313|EMBL:ACQ67582.1, ECO:0000313|Proteomes:UP000002334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AT {ECO:0000313|Proteomes:UP000002334};
RX   PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA   Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT   "Hamiltonella defensa, genome evolution of protective bacterial
RT   endosymbiont from pathogenic ancestors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
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; CP001277; ACQ67582.1; -; Genomic_DNA.
DR   RefSeq; WP_015873397.1; NC_012751.1.
DR   AlphaFoldDB; C4K4T9; -.
DR   STRING; 572265.HDEF_0862; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   GeneID; 66260696; -.
DR   KEGG; hde:HDEF_0862; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_2_7_6; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002334; Chromosome.
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, ECO:0000313|EMBL:ACQ67582.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          83..167
FT                   /note="Bifunctional transglycosylase second"
FT                   /evidence="ECO:0000259|Pfam:PF14814"
FT   DOMAIN          179..350
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          443..683
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   793 AA;  89165 MW;  E2405417100E3143 CRC64;
     MSHYGHEPIG QKNKKIHSKL HTSIKPKHSK KKWVFLRLLF ILFLSAGLVV ILYGFYLNEK
     IRQRIDGQVW VLPAAVYGRM LNLEPGMAYS KKQMINLLIA TQYRKVNHLL RVGEFTVQDN
     SIDMLRRPFN FPDAKEDQVH ARLLFHNDRL VQIENLDNQR FFGFFRLDPR LITMLQTPSG
     EQRLFLPRSS FPESLVNTLL AIEDRHFYQH DGINFYSIGR ALLANILAGR TVQGGSTLTQ
     QLVKNLFLNN QRSFWRKANE AYMAILIDHH YSKDKILELY FNEVYLGQNG NDQIRGFPLA
     SLYYFGRPVD ELSLDQQAML VGMVKGASLY NPWRNPEFTL ERRNLVLKLL QNQGNIDEKL
     YHTLSTRPLD VQPKGGVIVP QPAFIEMVRQ ELKQKLGDKA QHLSGAKIFT TMDPVSQDAA
     EKAIESGIPA LKGSEHDLSD LEGAMVVIDR LSGEIRAIVG GSQPQFSGFN RALQARRSIG
     SLAKPAIYLS ALNQPHQYRF NTWLFDQPLS LELPNGSVWE PKNYSRKFRG QVMLLDGLVD
     SLNVPTVNLG MSIGLDQISQ TMKQLGAPAS TGPLMPSMLL GAINLTPLEV AQEYQTIASG
     GNKATLSALR SVIAADGSML YQSFPQSERK LSAQASYLVL YGMQEAVKRG TARSLSSEFS
     TFHLAGKTGT TNDLRDSWFA GIDGKEVTII WLGRDNNGPT QFTGSTGALT LYRRYLETKP
     PLPLISRKPA GIVDMNIDST TGHFICDTEP HNQISTIPVW TEDPDVLCKT SEKTTPPNEL
     KEKSVLDSIK NIF
//