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Database: UniProt
Entry: G4QJG0_GLANF
LinkDB: G4QJG0_GLANF
Original site: G4QJG0_GLANF 
ID   G4QJG0_GLANF            Unreviewed;       777 AA.
AC   G4QJG0;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
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:AEP28566.1};
GN   OrderedLocusNames=GNIT_0412 {ECO:0000313|EMBL:AEP28566.1};
OS   Glaciecola nitratireducens (strain JCM 12485 / KCTC 12276 / FR1064).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Glaciecola.
OX   NCBI_TaxID=1085623 {ECO:0000313|EMBL:AEP28566.1, ECO:0000313|Proteomes:UP000009282};
RN   [1] {ECO:0000313|EMBL:AEP28566.1, ECO:0000313|Proteomes:UP000009282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 12485 / KCTC 12276 / FR1064
RC   {ECO:0000313|Proteomes:UP000009282};
RX   PubMed=22123761; DOI=10.1128/JB.06296-11;
RA   Bian F., Qin Q.L., Xie B.B., Shu Y.L., Zhang X.Y., Yu Y., Chen B.,
RA   Chen X.L., Zhou B.C., Zhang Y.Z.;
RT   "Complete genome sequence of seawater bacterium Glaciecola nitratireducens
RT   FR1064T.";
RL   J. Bacteriol. 193:7006-7007(2011).
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; CP003060; AEP28566.1; -; Genomic_DNA.
DR   RefSeq; WP_014107444.1; NC_016041.1.
DR   AlphaFoldDB; G4QJG0; -.
DR   STRING; 1085623.GNIT_0412; -.
DR   KEGG; gni:GNIT_0412; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_2_7_6; -.
DR   OrthoDB; 9766909at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000009282; 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:UP000009282};
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          62..136
FT                   /note="Bifunctional transglycosylase second"
FT                   /evidence="ECO:0000259|Pfam:PF14814"
FT   DOMAIN          165..333
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          429..668
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   ACT_SITE        188
FT                   /note="Proton donor; for transglycosylase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002799-1"
FT   ACT_SITE        466
FT                   /note="Acyl-ester intermediate; for transpeptidase
FT                   activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002799-1"
SQ   SEQUENCE   777 AA;  86445 MW;  33FFF9F965D299D8 CRC64;
     MKIKELPLLP FRWLKRHFWK LFIVALAASV SYVIYVDAQV KQRFEGNKWQ VPAQIFARPL
     TLQVKQEITI AEVKDELSLL GYRRVSAAKL TGEYQTYSNQ LRIQRRAFHF PNGYEPERDI
     RITWQGERIA KIEYLIGKGA NPTAKSIALT RLEPWLVSRL VSGLDEDRML VGKDDIPLLL
     QKALVIVEDR DFYQHHGVAP TSIIRAFFAN IVAGRTVQGG STLTQQLAKN FFLTRERSYI
     RKAKEAVMAV VIDARYSKEE IINAYINEVF LGQNGAVAVH GFGLASHFYF DKPLPELNTP
     EIATLIGLVK GPSFYSPSKH PERALERRNI VLRLLFEANE INSDEYAGFV AAPLNTASSE
     SLASGKHPAF MDKVRDELNA VISRRAEQLS GVKLYTTLDI NAQRRAEAAV KEQVDRIAQK
     REQPDLEAAM VVSDVQSGEI RAIVGGKKAG FSGFNRALNA YRPIGSLVKP AVYLSALEDP
     EHYNLATMLE DTPVKMRSTG GKYWEPLNSD KEFRGQVSLI EALTKSYNVP SVKLGMAVGL
     EEVAYTINRL GVDKEITLVP ALTLGAIDLS PLQVNQMYQT IANNGVMNQL HSLTAVTSNE
     NELLYLRDVE SEIRADESAT YLVNYALHKV TLEGTAKAVR EAFPNINMAG KTGTTNDYRD
     SWFAGFDRNL VTSVWMGSDD NAPVNLSGAS GAMQVFIAFQ KKQSPKNLSR RFPDGLGIAH
     FDAKTGELSA PGCGDILSVP AILSALPENA RGCDGQPAVR MQPKKKEKSF WEKLFGE
//
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