ID A0A101VPI3_9FIRM Unreviewed; 692 AA.
AC A0A101VPI3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Penicillin-binding protein {ECO:0000313|EMBL:KUO58253.1};
GN ORFNames=APF84_05290 {ECO:0000313|EMBL:KUO58253.1};
OS Gracilibacter sp. BRH_c7a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC Gracilibacter.
OX NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO58253.1, ECO:0000313|Proteomes:UP000053404};
RN [1] {ECO:0000313|EMBL:KUO58253.1, ECO:0000313|Proteomes:UP000053404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO58253.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
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 -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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:KUO58253.1}.
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DR EMBL; LOEZ01000091; KUO58253.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101VPI3; -.
DR STRING; 1734398.APF84_05290; -.
DR Proteomes; UP000053404; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 56..248
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 293..683
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 692 AA; 77021 MW; 335FBDA68E9143C1 CRC64;
MESMNRKESQ KRLTGLGIAV IIIFLILGFN LWRLQIANAS HYAELAASNV LKTVSTPAVR
GPIVDTNQVV MAQSVPKFAL VLDWADLQRV NKDLIDVVTN LAGYIKPYWH YPNQSIELIT
EDILVMVQNQ QRNNYDPVTI LVDIAPELQA IIAEHSNELP GVSIEAIAVR EYPQKTVLGQ
VLGYVREVSG TELEQFNQQA EDTDDPYRYE PGDLVGKDGI EKSYDKWLRG DHGLERIGID
SNARPIDKEV IQDAQPGNTV QLTVDSELQI VVENTLDEVI RNIQKTEPLA QAGAAVVIEV
NTGKILAMAS RPFMDPNELI GIISDETAER YFRTEDAASF NRALSGVYPP GSTFKMITGM
SALEAGVVTT NDYFNDSMSS LGPYEVQRQG IAEWGGNHFG MVNLYRGLAK SSNIYFQIVG
RRVFEKEPEL IKKIANEFGL AVPSGIDIPG EGVGVAPSPD WKRDYFKPYW DKLREDSLKE
IEDKYEKLLA DVTDESKRTG ILREKNREIS NVELDYKQKV DFYVNWRLFD SFNNSIGQGY
NSYTLVQLAN AVATMVNGGK LYKPYLVDKI YDTLTGEVIH ENVPEVRNEV SVSPETLEII
KKAMSGVTGG EGTANWLFWD VPQFSGGGKT GTAQIGSKNT AKGQFYNGMF VAFAPYDNPQ
IAYAGVVEFG GHGGETAGRV AKEAFIHYFN WK
//
