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Database: UniProt
Entry: A0A290XD23_9GAMM
LinkDB: A0A290XD23_9GAMM
Original site: A0A290XD23_9GAMM 
ID   A0A290XD23_9GAMM        Unreviewed;       822 AA.
AC   A0A290XD23;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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:ATD66983.1};
GN   ORFNames=CNR27_05610 {ECO:0000313|EMBL:ATD66983.1};
OS   Luteimonas chenhongjianii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Luteimonas.
OX   NCBI_TaxID=2006110 {ECO:0000313|EMBL:ATD66983.1, ECO:0000313|Proteomes:UP000218968};
RN   [1] {ECO:0000313|Proteomes:UP000218968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=100111 {ECO:0000313|Proteomes:UP000218968};
RA   Gui Z.;
RT   "Luteimonas liuhanmingii sp.nov., isolated from the intestinal contents of
RT   Tibetan Plateau Pika in Yushu, Qinghai Province, China.";
RL   Submitted (SEP-2017) 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; CP023406; ATD66983.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A290XD23; -.
DR   KEGG; lum:CNR27_05610; -.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000218968; 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; 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:UP000218968};
KW   Transferase {ECO:0000256|PIRNR:PIRNR002799};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..157
FT                   /note="Bifunctional transglycosylase second"
FT                   /evidence="ECO:0000259|Pfam:PF14814"
FT   DOMAIN          163..342
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          437..689
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          785..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..822
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        193
FT                   /note="Proton donor; for transglycosylase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002799-1"
FT   ACT_SITE        473
FT                   /note="Acyl-ester intermediate; for transpeptidase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002799-1"
SQ   SEQUENCE   822 AA;  89435 MW;  3CBD0D6C27260068 CRC64;
     MARIDYEDDD TDDPTEDAPP AWRRRVVTAV LALLALGLGF LIPYTIYLNH QVSEKFDALT
     WQVPTRVYAR PLQVTPGMAM NAATLKTELD AAGYREGDGV KPGTYATEGG RWTISSRGYR
     DVDRVVAPGR VQLTLSGGRV SRLRDGGGER ALEVARMDPA RIATLYGQRQ EERRLVRIDE
     VPPLLTDTLQ AVEDKDFAHH HGIDLSGMAR AAMVNLRAGE TRQGASTLTQ QLARSGLLGI
     GREQTYTRKF NEILYAMLIE ARYGKGPILE AYLNQVYLGQ RGAQAIHGVA AGAEFWFGRR
     LDDLEIEQVA LLVGIIRGPS YYDPRRHPER ALERRNFVLD KMLESGLIDQ AAHDRAIKRP
     LGVTETPGSI AANRFPAYVD LVRRQLARDY PAGDLQGAGL SVMSAMAPSA QAYAEGATVR
     TIKDLSTGKR PPLQAGLLVT DVHSGEVVAA VGSRDPVEHG FNRAVEAQRP VGSLLKPFVY
     LLALGNPTQY SLASWVDDSP VTITLENGRK WSPGNSDGRS HGTVRLIDAL ARSYNQATVR
     IGEAVGTRAL ADLVHVLAGV RATPNPSLTL GSMDQSPYAM AQLYQFLASG GEIQPLRSVR
     GVIDEQGRVL SRYDNAPRPA QEGDAIAARL VTIGLQEAVT SGTGRQLVND GLGRLNAAGK
     TGTSNDGRDS WFAGWTGDHL AVVWVGNDQN EQTGLYGATG AMRIWSGMFA RLPSAPLEVS
     NDGLEWKWIV QSNSTDADCP GARRFAFVSG YAPPYQPCRV YDPEQTFIDE NGNLVDATGA
     PVQQERRGWR EWFGFGRDEP EAPPAETAPS QPAPVPSPEE SP
//
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