ID A4NY56_HAEIF Unreviewed; 454 AA.
AC A4NY56;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Penicillin-binding protein 3 {ECO:0000313|EMBL:EDK13987.1};
GN ORFNames=CGSHiR3021_05764 {ECO:0000313|EMBL:EDK13987.1};
OS Haemophilus influenzae 22.4-21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=375063 {ECO:0000313|EMBL:EDK13987.1, ECO:0000313|Proteomes:UP000005596};
RN [1] {ECO:0000313|EMBL:EDK13987.1, ECO:0000313|Proteomes:UP000005596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22.4-21 {ECO:0000313|EMBL:EDK13987.1,
RC ECO:0000313|Proteomes:UP000005596};
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAZJ01000005; EDK13987.1; -; Genomic_DNA.
DR AlphaFoldDB; A4NY56; -.
DR BioCyc; HINF375063:G119K-1160-MONOMER; -.
DR Proteomes; UP000005596; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR Gene3D; 3.30.450.330; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022645};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000256|ARBA:ARBA00022645};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 3..84
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 124..415
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 454 AA; 49909 MW; 4CBAA9F8A59D13B7 CRC64;
MYLARQVELS KANYIRRLKI KGIILETEHR RFYPRVEEAA HVVGYTDIDG NGIEGIEKSF
NSLLVGKDGS RTVRKDKRGN IVAHISDEKK YDAQDVTLSI DEKLQSMVYR EIKKAVSENN
AESGTAVLVD VRTGEVLAMA TAPSYNPNNR VGVKSELMRN RAITDTFEPG STVKPFVVLT
ALQRGVVKRD EIIDTTSFKL SGKEIVDVAP RAQQTLDEIL MNSSNRGVSR LALRMPPSAL
METYQNAGLS KPTDLGLIGE QVGILNANRK RWADIERATV AYGYGITATP LQIARAYATL
GSFGVYRPLS ITKVDPPVIG KRVFSEKITK DIVGILEKVA IKNKRAMVEG YRVGVKTGTA
RKIENGHYVN KYVAFTAGIA PISDPRYALV VLINDPKAGE YYGGAVSAPV FSNIMGYALR
ANAIPQDAEA AENTTTKSAK RIVYIGEHKN QKVN
//
