ID A0A1Y0MPZ0_9FLAO Unreviewed; 622 AA.
AC A0A1Y0MPZ0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:ARV12436.1};
GN ORFNames=BTO09_08810 {ECO:0000313|EMBL:ARV12436.1};
OS Gilvibacter sp. SZ-19.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gilvibacter.
OX NCBI_TaxID=754429 {ECO:0000313|EMBL:ARV12436.1, ECO:0000313|Proteomes:UP000196054};
RN [1] {ECO:0000313|EMBL:ARV12436.1, ECO:0000313|Proteomes:UP000196054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZ-19 {ECO:0000313|EMBL:ARV12436.1,
RC ECO:0000313|Proteomes:UP000196054};
RA Kumagai Y., Yoshizawa S., Kogure K., Iwasaki W.;
RT "Trade-off between light-utilization and light-protection in marine
RT flavobacteria.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CP019333; ARV12436.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0MPZ0; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000196054; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000196054}.
FT DOMAIN 46..207
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 247..579
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 622 AA; 70711 MW; 071AAF38E0B08B4F CRC64;
MRKLLLLGLT LCSGLVFAAR LFYLQIYDSS FQKLSENNAI KMVYDYPERG YIFDRNGELM
VANQPAYDIM VIPRNVKDLD TLAFITDMGI TKEEFDRKLK KAWTYSPRIP SPFMPQLTKE
EFAALQEKMY QYKGFFIQKR SLRDYQVDHS ANVLGFIGEV NEAIMNRNPY YRLGDYIGMT
GVEKQYEDIL RGVKGVKYIQ KDRFNRDIGP YKDGIFDTIP VSGRDIVLTL DAELQAYGQL
LMQNKRGGIV AIEPKTGEIL SLITAPSYDP DYLVGRKRSK NYTGLYNDSI AKPLFDRVLE
GQYAPGSPFK ALTSLIGMQE GVVTAEERIS CSGAYYYGGR KPLGCHAHRS PLDMVGGIAN
SCNTYFCTIY RRTIEKYDSP QEGIDAWHDH LESFGLGNYM GYDLPSGRKG YIPDSGFYNR
SYNYPKYRWY ATATISNAIG QGEVTMTPMQ MAHTAAVIAN KGWFYRPHII KQIKGVDTLP
QKYTEKHYTT IDPEHFEPVI EGMFDVYNEG TAKFIQVPGI EICGKTGTAE NFMRIDGEVV
QLTDHSIFVA FAPKDDPKIA LAVFVENGYW GSRWAGRIAG LMIEKYLRGE ISRKDMEDFV
INGSLEEEYA KPFSGEPFII NQ
//
