ID A0A1N7RFL6_9BACT Unreviewed; 705 AA.
AC A0A1N7RFL6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:SIT33774.1};
GN ORFNames=SAMN05421788_113115 {ECO:0000313|EMBL:SIT33774.1};
OS Filimonas lacunae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Filimonas.
OX NCBI_TaxID=477680 {ECO:0000313|EMBL:SIT33774.1, ECO:0000313|Proteomes:UP000186917};
RN [1] {ECO:0000313|Proteomes:UP000186917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21054 {ECO:0000313|Proteomes:UP000186917};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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; FTOR01000013; SIT33774.1; -; Genomic_DNA.
DR RefSeq; WP_076382395.1; NZ_FTOR01000013.1.
DR AlphaFoldDB; A0A1N7RFL6; -.
DR STRING; 477680.SAMN05421788_113115; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000186917; 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, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186917};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..217
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 256..585
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 644..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 77934 MW; 3BF1C5B684679378 CRC64;
MPVYNQSRSR IVQIIFIVVF VVILGQLLHL QFFSSSYRMQ AENNARFRKV IYPDRGLIYD
RKEKAILGNT IMYDLVVTPG EIKGTDTFAL CKILGIDTAE FKKRIVGAII KNSTYKPSVF
EPLLSAELFA KLNENMYKFP GFILSDRPVR DYPFAAAANI LGYTGEVDTN FLKRHKEEGY
EMGDYAGMTG LERTYERVLM GTRGINYLTR DNRSRIQGKY ENGEYDTAAT AGKSLYSSID
IELQELGEKL MGNKVGSIVA IDPKTGGILC MVSSPTYNPN LLTGSQRRKH FSELYRDPRL
PLINRAVNGM YSPGSTFKTV VGIIGLTEGV IDENFTISCS GAFYGCGTGK PKCLDKGTFN
LTGAIAHSDN TYFATVFKRI LDQSRYGDAD SSLQVFNRYA YSFGLGKKLG VDIPSEKPGN
IPTPTYYQKI FGPKWVSCNI ISNAIGQGEV QTTITQLANV MALIANKGWY YTPHLIDSIE
GGDQYHLLDN YRVKHGISHV PEEVFNSVHN GMQGVMEYGT GQYAQVPGIV VCGKTGTVEN
YLRGVKQKDH AFFGAFAPRD NPRIAIAVMC ENAGFGSSSA APIASLMIEK YLNDSIAGKE
RKDKAEALAK LNLIPERMRR AMDSLARLTR TKDSIAQVKA QKAMADTLTM EEPTEGETGI
TNTMPADSNR PAKKDTSKKR TQAPPAILPP QKPKPKPAVP ATRTI
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