ID Q11GR9_CHESB Unreviewed; 574 AA.
AC Q11GR9;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Penicillin-binding protein, transpeptidase {ECO:0000313|EMBL:ABG63406.1};
GN OrderedLocusNames=Meso_2013 {ECO:0000313|EMBL:ABG63406.1};
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans.
OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG63406.1};
RN [1] {ECO:0000313|EMBL:ABG63406.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG63406.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000390; ABG63406.1; -; Genomic_DNA.
DR AlphaFoldDB; Q11GR9; -.
DR STRING; 266779.Meso_2013; -.
DR KEGG; mes:Meso_2013; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_2_5; -.
DR OrthoDB; 9789078at2; -.
DR GO; GO:0016020; C:membrane; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..184
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 250..548
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 574 AA; 62400 MW; 0584335D5B7C82EE CRC64;
MKLLPWRFKR SAPTAEQASI VLQGRRKATS GRAQSRIVLA MAMILGIYGA IGARLVHLGL
IEEAPVNLPQ TRPTASRPDL LDRNGEVLAT DIKTSSLFAE PRHIIDIDEV IEKLQKVLPD
LDYEQTYRRL DSDAGFVWLR RQLSPRQQSD ILALGIPGLG FRTEKTRFYP GGATASHILG
LVNIDNKGIA GMEQYVDDQG LADLQALGLA GPDTLEPVRL SIDLRAQYIL HDELSQAMDR
YHAIAAGGAI LNARTGEVVA MVSLPDYDPN NPYNALEKDR INRMTAGVFE MGSTFKLFTT
AMALDSGHVK MTDRFDASRP LRLGGFTIND FHGKGRVLSV PEVFIYSSNI GTAKMADVVG
IEGHRAFLKK VGLLDKMKTE LPEVAQPTEP KVWKKINSVT ISFGHGVATT PLQTAVSAVA
MVNGGKLIPP TFLPRTEEEA QAVATQVISP ETSAQIRYLF RLNVQKGTGG SGSRADVPGF
YVGGKTGTAE KVVNGRYSND KRFNAFLAAY PINDPEYVVV VILDEPKGEK PGMSATSGLN
AAPVVGNVIR RTAPLLGVEP DFSHESDALL VSYR
//
