ID A0A101WQV3_9FIRM Unreviewed; 592 AA.
AC A0A101WQV3;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Penicillin-binding protein transpeptidase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=APF77_03325 {ECO:0000313|EMBL:KUO77574.1};
OS Clostridia bacterium BRH_c25.
OC Bacteria; Bacillota; Clostridia.
OX NCBI_TaxID=1734399 {ECO:0000313|EMBL:KUO77574.1, ECO:0000313|Proteomes:UP000057710};
RN [1] {ECO:0000313|EMBL:KUO77574.1, ECO:0000313|Proteomes:UP000057710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c25 {ECO:0000313|EMBL:KUO77574.1};
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 -!- 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:KUO77574.1}.
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DR EMBL; LOES01000006; KUO77574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101WQV3; -.
DR STRING; 1734399.APF77_03325; -.
DR Proteomes; UP000057710; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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 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 PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF24; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE PBPA; 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 51..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 92..236
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 280..582
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 592 AA; 65708 MW; C82B98101483FD9E CRC64;
MSGILKFIKK TAVEEQKTEE ESNRAELLTL PGTRLYRKNN YMIIHKKRLK IIGISFILLY
MLMLGRLFYI QVYMGKEYSE RAVRQRMVHI PISANRGIIY DRNMIPITDR EIRKAVIAYP
AFVYDKKAAI DTISKACGIP RETVEKKMDG SVDTVEFICG VENNDYLSLI DSGRLKGVIA
VEKRLRYSDE DIARHVIGYI GKTDKIGHMG VEKSMNSYLE ASGSDSIAAV VDSGKNIIRG
LGFRKVDAPK DGQSYSIKLT LDYHIQNIIE RIMEDNDIQG SIVVMDVKNG DILGMASKPD
FDQDNLDKYL KSSGNELINK SIWQFDLGSI FKTVVAAAAI EGGFVNPYEK YKCEGYIDVG
NNRIKCSTYK SHEDREIDMI EAFALSCNST YIKIGTKTGA GEILEMAEKL GFGQKLCFTI
PEEKAGYIPT VQEDGIGNIS IGQGKIQATP LQITSMMATI ANNGIRNDPQ LVESLITEKG
LTVKKLERSR PQIVLNPITS KLLKEMLHEV TVTGTGKQAN MDEYGGSCGK TSSAQTGIDE
GEVVHGWFAG FVPYEKPQYA ITVFIYNGQS GGGAAAPIFK EAATEILKTV KR
//