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Entry: A0A0C4WK15_9GAMM
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Original site: A0A0C4WK15_9GAMM 
ID   A0A0C4WK15_9GAMM        Unreviewed;       780 AA.
AC   A0A0C4WK15;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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:AJE20306.1};
GN   ORFNames=Achr_8120 {ECO:0000313|EMBL:AJE20306.1};
OS   Azotobacter chroococcum NCIMB 8003.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=1328314 {ECO:0000313|EMBL:AJE20306.1, ECO:0000313|Proteomes:UP000068210};
RN   [1] {ECO:0000313|EMBL:AJE20306.1, ECO:0000313|Proteomes:UP000068210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 8003 {ECO:0000313|EMBL:AJE20306.1,
RC   ECO:0000313|Proteomes:UP000068210};
RX   PubMed=26061173;
RA   Robson R.L., Jones R., Robson R.M., Schwartz A., Richardson T.H.;
RT   "Azotobacter Genomes: The Genome of Azotobacter chroococcum NCIMB 8003
RT   (ATCC 4412).";
RL   PLoS ONE 10:E0127997-E0127997(2015).
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; CP010415; AJE20306.1; -; Genomic_DNA.
DR   RefSeq; WP_039802109.1; NZ_CP010415.1.
DR   AlphaFoldDB; A0A0C4WK15; -.
DR   STRING; 1328314.Achr_8120; -.
DR   KEGG; acx:Achr_8120; -.
DR   HOGENOM; CLU_006354_2_7_6; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000068210; 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   Reference proteome {ECO:0000313|Proteomes:UP000068210};
KW   Transferase {ECO:0000256|PIRNR:PIRNR002799};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          69..151
FT                   /note="Bifunctional transglycosylase second"
FT                   /evidence="ECO:0000259|Pfam:PF14814"
FT   DOMAIN          163..334
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          426..665
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   ACT_SITE        187
FT                   /note="Proton donor; for transglycosylase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002799-1"
FT   ACT_SITE        463
FT                   /note="Acyl-ester intermediate; for transpeptidase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002799-1"
SQ   SEQUENCE   780 AA;  85561 MW;  999ED83B5063B1DA CRC64;
     MTRTRSPKSP SPRRSGALRS WLGWTAKLAL VGLVVLAGFA VYLDAVVQEK FSGKRWTLPA
     KVYARPLELF SGLKLSKQDF LTELDALGYR REAVAGPGSA AVSGNTVDLH TRGFRFYEGD
     EPARRIRVRF SGDYVAGLSG ADGSDLPVVR MEPLLIGGLY PAHNEDRILV QRNELPPYLV
     ETLVAVEDRE FFSHFGVSPK SIVRALWVNA AAGGVVQGGS TLTQQLVKNF YLSNERSLVR
     KATEAMMAVL LELHYDKDEI LEAYLNEVFL GQDGNRAVHG FGLASQYFFG QPLAELQPHQ
     VALLVGMVKG PTYYNPRRNP ERAMTRRNLV IDLMAEQSVI DAAQAAAAKQ KPLGVTARGS
     LANSAHPAFL DLVKRQLRED YQEADLTEEG LRIFTSLDPI LQNKAEAAVH DTFKRIGKGG
     DPVEASMVVS NPETGEVLAL LGSRQPRFAG FNRALDAVRP IGSLIKPAIY LTALEKPSQY
     TLTSWVADVP FSVKGQDGQL WRPQNYDHQA HGDIYLYQGL ANSYNLSTAK LGLELGVPNV
     LKTLARLGVE REWPAYPSML LGAGALTPME VSSMYLTIAS GGFNTPLRGI RSVLDSAGEP
     LKRYPFQIQQ RFDPGAIYLL QNAMQRVMRE GTGRSVYSRL PRSLNLAGKT GTTNDSRDSW
     FAGFSQDLLA VVWLGRDDNG KTPLTGATGA LRVWTDFMAK ADPLPLDMPV PDNVTEVWVN
     ARNGLGSEPG CPDTVQMPYI RGSEPPPGPP CGLPQAPAEN VQDVIENVQD VMDWVRDWSN
//
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