ID A0A101CW64_9FLAO Unreviewed; 654 AA.
AC A0A101CW64;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:KUJ63325.1};
GN ORFNames=AR687_04020 {ECO:0000313|EMBL:KUJ63325.1};
OS Flavobacteriaceae bacterium CRH.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1742859 {ECO:0000313|EMBL:KUJ63325.1, ECO:0000313|Proteomes:UP000053826};
RN [1] {ECO:0000313|EMBL:KUJ63325.1, ECO:0000313|Proteomes:UP000053826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRH {ECO:0000313|EMBL:KUJ63325.1,
RC ECO:0000313|Proteomes:UP000053826};
RA Newman J.D., Miller J.R., Jacobs K.T.;
RT "Genome Sequence of Flavobacterium sp. CHR.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:KUJ63325.1}.
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DR EMBL; LMAJ01000003; KUJ63325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101CW64; -.
DR STRING; 1742859.AR687_04020; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000053826; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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 InterPro; IPR017790; Penicillin-binding_protein_2.
DR NCBIfam; TIGR03423; pbp2_mrdA; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 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}.
FT DOMAIN 46..210
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 248..577
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 654 AA; 73157 MW; D1AE3A6AF22734D0 CRC64;
MRKVLLPSLI IIAASLLVMR IFYLQIIDDS FKLKSENNAI KKAYDYPERG YIYDRNGKLL
VANQASYDIM VIPREIKKDL NVTEFCNLLS ITPEEYYKRI AKAKVYSPRL PSVFLAQLNK
SEFAAFQEKI RKYEGFYFQK RSLRDYEVDY GANIFGFITQ VNEGLIAKNP YYNSGDLIGM
QGVEQSYEEV LRGIKGVKYI QKDKYNREIG SYKEGKYDTI AVAGEDINLT IDAELQKYGE
ELMINKRGGI VAIEPKSGEI LALITAPSYD PGILVGRQRS KNYTLLYHDS IAKPLYDRGL
LAEYPPGSPF KILTGLVALQ EGVIDEQTTF MCHHGFSYGR GRFMKCHGFG PHQLHNGIYN
SCNTYFAQSY MLTINKYGDP GKAVDVWSNH VKSFGLGQFM GYDLPTGKKG NIPTSKTYKK
IYPNGGWRST TIVSNAIGQG EVLMTPIQLA NMMATVANQG YYYTPHIIKK IEGKKIDAKF
TTKHETTIDK KYFPPVISGL FDVYNKGTAY ALRVEGIDIC GKTGTAENYA KIGGVRTKLK
DHSIFVAFAP KDNPKIAIAI MIENGGFGAT VAGPIASLMI EKYLRKKITR NDLEVRVLNK
SLASEYAKLG GMTDASAIES TPKDSVLKAK IVVPKVPIAP KTEIKKTTVD TTKN
//
