ID A0A143WSW9_9ENTR Unreviewed; 792 AA.
AC A0A143WSW9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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:CUX96884.1};
GN ORFNames=MHIR_DE00650 {ECO:0000313|EMBL:CUX96884.1};
OS Candidatus Doolittlea endobia.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Doolittlea.
OX NCBI_TaxID=1778262 {ECO:0000313|EMBL:CUX96884.1, ECO:0000313|Proteomes:UP000095322};
RN [1] {ECO:0000313|Proteomes:UP000095322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Husnik F.;
RL Submitted (JAN-2016) 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; LN999833; CUX96884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143WSW9; -.
DR STRING; 1778262.MHIR_DE00650; -.
DR KEGG; den:MHIR_DE00650; -.
DR PATRIC; fig|1778262.3.peg.1184; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000095322; Chromosome i.
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; IPR027417; P-loop_NTPase.
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.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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:UP000095322};
KW Transferase {ECO:0000256|PIRNR:PIRNR002799};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..149
FT /note="Bifunctional transglycosylase second"
FT /evidence="ECO:0000259|Pfam:PF14814"
FT DOMAIN 161..331
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 425..664
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 792 AA; 88348 MW; EBA15FE33FB5F27C CRC64;
MPLRKEKEGV PQKKCCLLGR LVCLLPLLVV VVAIYGVYLD TQVRHRIDGK VWQLPAVVYS
RMINLEPGVS YSRSNMATLL VGMQYREVSR ISRPGEFTIR GNSIELLRRP FDFPDNKEGQ
IHVRMTFTKN QLLEIKNQET GRNFGVFRLD PRLIAMLQSP KGEQRLFVPR NGFPDLLVDT
LIATEDRHFY QHDGISLSSI CRAFLANIIA GRTVQGGSTL TQQLVKNLFL INERSLWRKA
NEAYIALIVD HRYSKDRVLE LYMNEVYLGQ NGSDQIRGFP LASLYYFGRP VDELSLDQQA
MLVGMVKGAS LYNPWRNPKL ALERRNLVLK LLEKQKIIDN KLYNILSARQ LKVQPRGGIL
TPQPAFMQMV REELQSKLGD KINDLSGVKI FTTLDPLSQD AAEKALEIGI PALRASRGIK
DLEAAMVVVD RFSGEVRAMV GGSEPQFAGF NRAMQARRSV GSLAKPATYL TALSDPDKYR
LNTWIPDEPI TLKQPNGRLW SPKNYDRRFR GKVMLVDALT KSLNVPTVNL GLSVGLDRLT
ATLMKLGVPS SGLNPVPSML LGAISLTPIE VAQEFQTIAS GGNHATLSAV RSVIGEDGAV
LFQSLPQSER VLPAQAAYLT LYAMQQVVVR GTSRSLSVQF PSSHLAAKTG TTNDLRDSWF
VGIDGKEVSI SWVGRDNNGP AKLSGANGAL TLYRRYLEKQ APLTLHLTPP EGISQIPIDY
AGNFVCNGGS EMRTLPVWTD NPQSLCQLTQ MQVQQQIDTD APVEKSQQHL ILQDKKKDGN
GVTNWIWRIF SK
//
