ID F8E2I0_CORRG Unreviewed; 593 AA.
AC F8E2I0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:AEI08626.1};
DE EC=2.4.2.- {ECO:0000313|EMBL:AEI08626.1};
GN Name=pbp2B {ECO:0000313|EMBL:AEI08626.1};
GN OrderedLocusNames=CRES_0263 {ECO:0000313|EMBL:AEI08626.1};
OS Corynebacterium resistens (strain DSM 45100 / JCM 12819 / GTC 2026 / SICGH
OS 158).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=662755 {ECO:0000313|EMBL:AEI08626.1, ECO:0000313|Proteomes:UP000000492};
RN [1] {ECO:0000313|EMBL:AEI08626.1, ECO:0000313|Proteomes:UP000000492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45100 / JCM 12819 / GTC 2026 / SICGH 158
RC {ECO:0000313|Proteomes:UP000000492};
RX PubMed=22524407; DOI=10.1186/1471-2164-13-141;
RA Schroder J., Maus I., Meyer K., Wordemann S., Blom J., Jaenicke S.,
RA Schneider J., Trost E., Tauch A.;
RT "Complete genome sequence, lifestyle, and multi-drug resistance of the
RT human pathogen Corynebacterium resistens DSM 45100 isolated from blood
RT samples of a leukemia patient.";
RL BMC Genomics 13:141-141(2012).
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP002857; AEI08626.1; -; Genomic_DNA.
DR RefSeq; WP_013887654.1; NC_015673.1.
DR AlphaFoldDB; F8E2I0; -.
DR STRING; 662755.CRES_0263; -.
DR KEGG; crd:CRES_0263; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_025328_0_0_11; -.
DR OrthoDB; 5241017at2; -.
DR Proteomes; UP000000492; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:AEI08626.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000492};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:AEI08626.1}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..593
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038957421"
FT DOMAIN 311..555
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 593 AA; 64024 MW; 9E6754D0A056671E CRC64;
MMTKHNRFRQ SVIALCSLSA VMLSSCSALP WESDSDVFLK AFNAGDDSKA ARYLDHPDPE
RALHEFRQSL HGVKVNIEKS DISNGKQNTH VTWSKDGVEL ESNGRLVLSG QDGKPQWLPS
IFEAQLSDDS ALFFAEDKQY DLPIKDRLGN EYMTWTKVIQ VRGRKDIASR AQELAQIFAQ
VSPTTTKEWI EQTLGESQDE DTVLLTLRQE EFRKIQEQLR TFEGISTVEQ GRLLSVSKTL
NSPLDAELNK YWESVLDANS GWSIRAESSQ GMTTVASEPP RRVQPIATTL DNTLQSAAKQ
AVDSEQRAAV LVVLNPRTGG VLAVAQNDKA NNQGPIALTG LFPPGSTFKT VTTAAALEAG
AVSMDEELPC PSNITVAGRK IPNDHDFDLG SVRLEEAFAQ SCNTTQAVIS DRLGEDDLQR
TALELGIGSD FDVPGMTTLT GSVPRTPAGP PRVEASIGQG EVLASPFGIA LMQSTVANGG
LLVPPQLIQG EQTVVNKQAD QHVSDTTIQS LRTMMKSTID HGSARSLSDL SALGGKTGTA
EIDGKLSNGW FAGTTGELAI ASLVIEGDSS QPAVEMAGRF LRSPDVQKFS GIQ
//
