ID D3UJ25_HELM1 Unreviewed; 586 AA. AC D3UJ25; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAR-2024, entry version 57. DE SubName: Full=Putative penicillin-binding protein {ECO:0000313|EMBL:CBG40500.1}; GN Name=pbpB {ECO:0000313|EMBL:CBG40500.1}; GN OrderedLocusNames=HMU12460 {ECO:0000313|EMBL:CBG40500.1}; OS Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 / 12198) OS (Campylobacter mustelae). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=679897 {ECO:0000313|EMBL:CBG40500.1, ECO:0000313|Proteomes:UP000001522}; RN [1] {ECO:0000313|EMBL:CBG40500.1, ECO:0000313|Proteomes:UP000001522} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43772 / LMG 18044 / NCTC 12198 / 12198 RC {ECO:0000313|Proteomes:UP000001522}; RX PubMed=20219135; DOI=10.1186/1471-2164-11-164; RA O'Toole P.W., Snelling W.J., Canchaya C., Forde B.M., Hardie K.R., RA Josenhans C., Graham R.L.J., McMullan G., Parkhill J., Belda E., RA Bentley S.D.; RT "Comparative genomics and proteomics of Helicobacter mustelae, an RT ulcerogenic and carcinogenic gastric pathogen."; RL BMC Genomics 11:164-164(2010). 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; FN555004; CBG40500.1; -; Genomic_DNA. DR RefSeq; WP_013023568.1; NC_013949.1. DR AlphaFoldDB; D3UJ25; -. DR STRING; 679897.HMU12460; -. DR KEGG; hms:HMU12460; -. DR eggNOG; COG0768; Bacteria. DR HOGENOM; CLU_009289_6_4_7; -. DR Proteomes; UP000001522; Chromosome. 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 Reference proteome {ECO:0000313|Proteomes:UP000001522}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 12..31 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 49..226 FT /note="Penicillin-binding protein dimerisation" FT /evidence="ECO:0000259|Pfam:PF03717" FT DOMAIN 268..573 FT /note="Penicillin-binding protein transpeptidase" FT /evidence="ECO:0000259|Pfam:PF00905" SQ SEQUENCE 586 AA; 65523 MW; 2096E79859BB7D80 CRC64; MNEQSGRIVK VFSVFVVFII IALLLCLFTL GKILGPNHIP FWQSKRIQVA TRGSIYSDDN FDLASSQVLY KVSINTLSID PDKRELFINL FSIYSGMSRE ELQAKLKQKG YIVFSYNIPA NVAANLRQLR SKLLAYDVFR EYQDSSGRIV QKMGIDVEVS GINRNYAYND ALEPVLGYVK KREARSVTIP EGVKGLEKYY NKELSPKQNG IERGDRDIRG NIIRNKTTIL RERINGSDIA LHVNLGLQRK VEKMLDEFYQ QYQVDEIVAG VMDPKSGAIF ALATTNRFDP KNITSNHALN ASVTERPFEP GSTIKPIVFS ILLDKNLINP LELIDLNKGF LQLGRYTIKD DIYPKKNSIV QDILIRSSNV GMIKISRKLS GKEFYEGLKS FGISEASGID LPYERDGVIP SIRKLSGEAY KASASYGYGL TTTFIQLLRA YGVFCNNGIL VTPHLIKNIT DPDGKITTPT FPTRQAIAAP TARKIQEILI KTVQEGTGKR AKIDNLIVGG KTGTARIAKS GGGYSDNIYN GSFFGFVKGG NQTYVIGVVV FGTQHKEDYY GSQTAAPIFK EIARIMQKQN FFKEQK //