ID M7S3N8_SALDU Unreviewed; 840 AA.
AC M7S3N8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=A670_02090 {ECO:0000313|EMBL:EMR52781.1};
OS Salmonella enterica subsp. enterica serovar Dublin str. UC16.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1192688 {ECO:0000313|EMBL:EMR52781.1, ECO:0000313|Proteomes:UP000013259};
RN [1] {ECO:0000313|EMBL:EMR52781.1, ECO:0000313|Proteomes:UP000013259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC16 {ECO:0000313|EMBL:EMR52781.1,
RC ECO:0000313|Proteomes:UP000013259};
RA McClelland M., Porwollik S., Desai P., Cheng P., Wollam A., Pepin K.,
RA Bhonagiri V., Fulton L., Fulton R., Delehaunty K., Fronick C., Godfrey J.,
RA Waligorski J., Appelbaum E., Tomlinson C., Warren W., Sodergren E.,
RA Weinstock G., Wilson R.K.;
RL Submitted (FEB-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:EMR52781.1}.
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DR EMBL; APMR01000035; EMR52781.1; -; Genomic_DNA.
DR RefSeq; WP_000918129.1; NZ_KB731409.1.
DR AlphaFoldDB; M7S3N8; -.
DR PATRIC; fig|1192688.3.peg.2003; -.
DR HOGENOM; CLU_006354_2_7_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000013259; 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; IPR032730; PBP1b_TM.
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; PF14812; PBP1_TM; 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 60..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..74
FT /note="Transglycosylase PBP1b N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF14812"
FT DOMAIN 108..192
FT /note="Bifunctional transglycosylase second"
FT /evidence="ECO:0000259|Pfam:PF14814"
FT DOMAIN 204..374
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 468..709
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..821
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 93840 MW; CE43FAB379DBA14B CRC64;
MAGNDREPIG RKGKPSRPVK QKVSRRRQHD DDYDDDYEDE EPMPRKGKGK GRKPRGKRGW
LWLLLKLFIV FVVLFAIYGV YLDQKIRSRI DGKVWQLPAA VYGRMVNLEP DMPVSKNEMV
KLLEATQYRL VTKMTRPGEF TVQANSIEMI RRPFDFPDSK EGQVRARLTF SDGRLETIVN
LDNNRQFGFF RLDPRLITML SSPNGEQRLF VPRSGFPDLL VDTLLATEDR HFYEHDGISL
YSIGRAVLAN LTAGRTVQGA STLTQQLVKN LFLSSERSYW RKANEAYMAL IMDARYSKDR
ILELYMNEVY LGQSGDNEIR GFPLASLYYF GRPVEELSLD QQALLVGMVK GASIYNPWRN
PKLALERRNL VLRLLQQQKI IDQELYDMLS ARPLGVQPRG GVISPQPAFM QMVRQELQAK
LGDKIKDLSG VKIFTTFDSV AQDAAEKAVV EGIPALKKQR KLSDLETAMV VVDRFSGEVR
AMVGGAEPQY AGYNRAMQAR RSIGSLAKPA TYLTALSQPN LYRLNTWIAD APISLRQPNG
QVWSPQNDDR RYSESGKVML VDALTRSMNV PTVNLGMALG LPAVTDTWTK LGVPKDQLNP
VPAMLLGALN LTPIEVAQAF QTIASGGNRA PLSALRSVIA EDGKVLYQSY PQAERAVPAQ
AAYLTLWTMQ QVVQRGTGRQ LGAKYPGLHL AGKTGTTNNN VDTWFAGIDG SQVTITWVGR
DNSQPTKLYG ASGAMAIYQR YLANQTPTPL VLTPPEDVVD MGVDYDGNFV CSGGMRTLPV
WTDDPNTLCQ QGEMMQQQQQ PSGNPFDQSS QPQQPAQQQP PKEEKSDGVA GWIKEMFGGN
//
