ID A0A0B3VSV4_9FIRM Unreviewed; 667 AA.
AC A0A0B3VSV4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Penicillin-binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=QX51_17940 {ECO:0000313|EMBL:KHS55699.1};
OS Terrisporobacter othiniensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Terrisporobacter.
OX NCBI_TaxID=1577792 {ECO:0000313|EMBL:KHS55699.1, ECO:0000313|Proteomes:UP000031189};
RN [1] {ECO:0000313|EMBL:KHS55699.1, ECO:0000313|Proteomes:UP000031189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=08-306576 {ECO:0000313|EMBL:KHS55699.1,
RC ECO:0000313|Proteomes:UP000031189};
RA Lund L.C., Sydenham T.V., Hogh S.V., Skov M.N., Kemp M., Justesen U.S.;
RT "Draft genome sequence of Terrisporobacter sp. 08-306576, isolated from the
RT blood culture of a bacteremia patient.";
RL Submitted (DEC-2014) 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:KHS55699.1}.
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DR EMBL; JWHR01000153; KHS55699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B3VSV4; -.
DR STRING; 1577792.QX51_17940; -.
DR Proteomes; UP000031189; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; 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; IPR007887; MecA_N.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR30627:SF25; PENICILLIN-BINDING PROTEIN 3; 1.
DR PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR Pfam; PF05223; MecA_N; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF54427; NTF2-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000031189}.
FT DOMAIN 31..145
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 153..305
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 348..660
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 667 AA; 74096 MW; 627A31A943E4CDE2 CRC64;
MKKLSRLVIV SMMIISVFIL SGCSDKNEMK NTVKNYTKLL NEKKYDELYE ILTTDSKEYI
KEEFGGKEGF VNKYSAIYSA MGVNNIKIDV GEIKDKSEIP ITISMNTIGG KLKYEDAIIK
LKKEDDKYKI CWNESLILPD MVQGDKIRVK VSNGNRGEIL DRDGNLLAYN GEVNYINIDP
KLFKKEDISD LAKALDISEE YIEKKIENNI NPDYAINIVK VSKYEEDKVQ EALKIEGVMS
QVGASRVYAK GEAFGSLLGY IGDITAEELE KNAGKGYTTS SQVGKNGLEQ VYEDTLRATD
GVHIYIERGG EDITLAKIKS SDGKDIKLAI DSDLQKSVYD QMDNEKGASI AMNSATGEVL
AMVSSPSYDS NTMVTYKTKT IAKEWEENKN ASFDNRANNL YSPGSTMKLI TASIGIENKE
IDPNEKMKIE GVNWQKSSSW GNYKVTRVKN VSSVNLYDAV VNSDNIYFAD KAIKIGSENL
IEGAKKFGLG ADIKFEYPMS NSQISNSGAI DSEILLGDTG YGQGEVLTTP LQITMAYSAL
GNEGKIMTPR LVLSENKEEK VYSEAIQKKY LKELQKDFAG VINDSNGSGY LCKIEGVNLA
GKTGTAEIKS TKEDETGNEN SWFVAVDMDN SKLAISMVME NMKYKSTSKY LVPKVKNIMK
SYISEDK
//