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Database: UniProt
Entry: A0A101WQV3_9FIRM
LinkDB: A0A101WQV3_9FIRM
Original site: A0A101WQV3_9FIRM 
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
//
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