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Database: UniProt
Entry: Q65R28_MANSM
LinkDB: Q65R28_MANSM
Original site: Q65R28_MANSM 
ID   Q65R28_MANSM            Unreviewed;       873 AA.
AC   Q65R28;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 111.
DE   RecName: Full=Penicillin-binding protein 1A {ECO:0000256|ARBA:ARBA00018638};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE            EC=3.4.16.4 {ECO:0000256|ARBA:ARBA00012448};
GN   Name=mrcA {ECO:0000313|EMBL:AAU38582.1};
GN   OrderedLocusNames=MS1975 {ECO:0000313|EMBL:AAU38582.1};
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988 {ECO:0000313|EMBL:AAU38582.1, ECO:0000313|Proteomes:UP000000607};
RN   [1] {ECO:0000313|EMBL:AAU38582.1, ECO:0000313|Proteomes:UP000000607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E {ECO:0000313|EMBL:AAU38582.1,
RC   ECO:0000313|Proteomes:UP000000607};
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00034000};
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}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004249}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004249}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC       family. {ECO:0000256|ARBA:ARBA00007090}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR   EMBL; AE016827; AAU38582.1; -; Genomic_DNA.
DR   RefSeq; WP_011201133.1; NC_006300.1.
DR   AlphaFoldDB; Q65R28; -.
DR   STRING; 221988.MS1975; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   KEGG; msu:MS1975; -.
DR   eggNOG; COG5009; Bacteria.
DR   HOGENOM; CLU_006354_2_4_6; -.
DR   OMA; QQNTGGD; -.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000607; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 3.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR031376; PCB_OB.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF27; PENICILLIN-BINDING PROTEIN 1A; 1.
DR   Pfam; PF17092; PCB_OB; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT   DOMAIN          55..229
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          318..413
FT                   /note="Penicillin-binding protein OB-like"
FT                   /evidence="ECO:0000259|Pfam:PF17092"
FT   DOMAIN          417..650
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          619..659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        626..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   873 AA;  96441 MW;  2FA81FE8A83FBF48 CRC64;
     MKIVKLIFST LLTIVILGCV AGGLLYFHIK SQLPDVQSLK TVELQQPMQI YTADEKLIGE
     VGEQRRIPVK LENVPKMLIN AILATEDSRF YEHHGLDPVG IARAVSVAIA NKGASQGAST
     ITQQLARNFF LTPEKTIIRK TKEAILAIEI ENTLTKNEIL ELYLNKIYLG YRSYGVAAAA
     KTYFGKNLAD LTLSEMAIIA GLPKAPSTMN PLYSLKRSEE RRNVVLGRML EMQFINKEQY
     DEAVQEPIKA SYHGAQIEFR ADYVTEMVRQ EMVKRYGEES AYNSGFKVYT TILSQDQAQA
     QKAVRNNLID YDMRHSRYRG ATPLWQSSET PWENNKIIDT LRKLPNSEPF LPAVILSVAK
     EGTELLLASG EKMTLNAAAM RWGGRNVSLK TGEQIWIRQR DNNEWVLGQI PEANSALVSL
     NSDNGAIEAI VGGFSFEQSK FNRATQSMVQ VGSSIKPFIY AAALEKGLTL SSVLQDTPIS
     IRKPGQAEWR PKNSPDRYDG PMRLRVGLGQ SKNMIAIRAM QTAGIPYVAE FLQRFGFKRE
     QYFASEALAL GAASFTPLEM ARGYAVFDNG GFLVDPFIIN RIVDNSGKDI FIANPKIACT
     TCDEMPTIYG QTTDKVDGFK ENDSVNADGN LAQTDENTNG EETDQNGENN DVPELQNQGG
     TINEDALNLM VEGKTDSSQV QYAPRVITGE LAFLIRSALN TAIYGEQGLG WKGTSWRMAN
     EIKRKDIGGK TGTTNNAKVA WYAGFGANLT TAVYVGFDDN KRNLGKGEAG AKTAMPAWIN
     YMKFVLEDVP ERVLPTPANI IEKSIDLGSG LLSKGGGRTE YFIKGTEPKR AFVQERGYYV
     PEGLPFQTPS ASEYVPIGQP APAAPAPSRK ELF
//
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