ID F9GQP1_HAEHA Unreviewed; 792 AA.
AC F9GQP1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:EGT74605.1};
GN ORFNames=GG9_1536 {ECO:0000313|EMBL:EGT74605.1};
OS Haemophilus haemolyticus M19501.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1028803 {ECO:0000313|EMBL:EGT74605.1};
RN [1] {ECO:0000313|EMBL:EGT74605.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M19501 {ECO:0000313|EMBL:EGT74605.1};
RX PubMed=21952546; DOI=10.1128/JB.05863-11;
RA Jordan I.K., Conley A.B., Antonov I.V., Arthur R.A., Cook E.D.,
RA Cooper G.P., Jones B.L., Knipe K.M., Lee K.J., Liu X., Mitchell G.J.,
RA Pande P.R., Petit R.A., Qin S., Rajan V.N., Sarda S., Sebastian A.,
RA Tang S., Thapliyal R., Varghese N.J., Ye T., Katz L.S., Wang X., Rowe L.,
RA Frace M., Mayer L.W.;
RT "Genome Sequences for Five Strains of the Emerging Pathogen Haemophilus
RT haemolyticus.";
RL J. Bacteriol. 193:5879-5880(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGT74605.1}.
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DR EMBL; AFQO01000015; EGT74605.1; -; Genomic_DNA.
DR RefSeq; WP_005632610.1; NZ_AFQO01000015.1.
DR AlphaFoldDB; F9GQP1; -.
DR PATRIC; fig|1028803.3.peg.1607; -.
DR eggNOG; COG0744; Bacteria.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000003258; Unassembled WGS sequence.
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; TIGR02074; PBP_1a_fam; 1.
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 Transferase {ECO:0000256|PIRNR:PIRNR002799};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..153
FT /note="Bifunctional transglycosylase second"
FT /evidence="ECO:0000259|Pfam:PF14814"
FT DOMAIN 158..335
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 428..669
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 751..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 89555 MW; 0784FFB26079F3A9 CRC64;
MTTENVPKNP EEKTPKKRCS FRNFLLKVAF TGAVLTVFYG GYLDWQIRSK MDGQIWRLPA
EVYSRIESVK ISDNLAFDEV IQILLDNEYR QTTMVAAPGD FKLEDDTIVV LRRAFPFPDK
AEPQRVLRLR FNNNKLSRIE DLVTVKTVDE FRLAPKLIAM LQSDNEDRLA IPLQNYPRLL
IDTLILTEDR RFYEHNGINP VGIFRALIAN IRAGQTVQGG STLTQQLVKN LFLSRERTIT
RKANEALMSL VLDWRYDKNR ILETYLNEIY LGQNGDTQIH GFELASQFYF GRSIREISLD
QIALLVGMVK GPSLYNPWRN PQNALERRNI VLKLMLEHKM IGDELYQLLS QRPLGVQKKG
QISRKYPAFI QTLQADLRRE LGEHKISSLL GARIFTTMDL KQQSQAENAV VNTVSQLQLK
TKNPYLEGAM IVADYRVGEI RAVVGGLQTQ YAGFNRALMA KRQIGSLVKP SIYLTALSNP
EQFRLNTPIN NQPITINVKG SPPWQPRNYD KKYSGSVMLM DALARSLNIP TVNIGMKVGL
SKIINTQKAM GWDNVEIPKV PAMLLGSYTI SPYDVTKLYQ TIANQGGRIS LTTVDSITDR
QGNLIFQHDK SVKQVVPQEA AFQTLFAMQQ TVERGTARSL QKDYADLHLA GKTGTTNEAR
DTWFVGIDGK NISTVWLGRD DNGETKLTGA SGALQIYKDY LSRTNIEKLA IKPPATVKWV
GINQYGGWDC ESYRTIPVWL NNGQNFCGEI ASPSFTPTET ETETETETET ETTTPPQESL
WDVLDNPNPP AQ
//
