ID A0A0S2VZT4_9FIRM Unreviewed; 709 AA.
AC A0A0S2VZT4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Penicillin-binding protein 2 (PBP-2) {ECO:0000313|EMBL:ALP92619.1};
GN ORFNames=IB211_00223 {ECO:0000313|EMBL:ALP92619.1};
OS Intestinimonas butyriciproducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Intestinimonas.
OX NCBI_TaxID=1297617 {ECO:0000313|EMBL:ALP92619.1, ECO:0000313|Proteomes:UP000064844};
RN [1] {ECO:0000313|EMBL:ALP92619.1, ECO:0000313|Proteomes:UP000064844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF211 {ECO:0000313|EMBL:ALP92619.1,
RC ECO:0000313|Proteomes:UP000064844};
RX PubMed=26620920; DOI=10.1038/ncomms10062;
RA Bui T.P., Ritari J., Boeren S., de Waard P., Plugge C.M., de Vos W.M.;
RT "Production of butyrate from lysine and the Amadori product fructoselysine
RT by a human gut commensal.";
RL Nat. Commun. 6:10062-10062(2015).
RN [2] {ECO:0000313|Proteomes:UP000064844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF211 {ECO:0000313|Proteomes:UP000064844};
RA de Vos W.M., Bui N.T.P., Plugge C.M., Ritari J.;
RT "A butyrogenic pathway from the amino acid lysine in a human gut
RT commensal.";
RL Submitted (APR-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}.
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DR EMBL; CP011307; ALP92619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S2VZT4; -.
DR STRING; 1297617.IB211_00223; -.
DR KEGG; ibu:IB211_00223; -.
DR PATRIC; fig|1297617.4.peg.225; -.
DR eggNOG; COG0768; Bacteria.
DR Proteomes; UP000064844; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 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: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};
KW Reference proteome {ECO:0000313|Proteomes:UP000064844}.
FT DOMAIN 61..313
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 368..685
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 709 AA; 78098 MW; E829E7AEA75EE026 CRC64;
MNGKKEPMMD GRQFHVRVRG VMVLLAAVLV GFLWVLYDLQ YVHGAEYLEQ SRRKIAKTET
VEASRGQILD RYGRVLVGNR ASYNVSLDTS FMGEDRNTVL LRLLDICREE SVTWSDTLPV
SRSAPYVFTA EGAYGNLRKY AEKMKWDGLV PTAEELEALQ SAESPALPSA ERLLAKLRET
YQVDPALSDG EARDLVGVLY ELALRSREIT WSSYVFAQDV EMAFIVKVKE ASLSGVSIDT
TTVREYNTSY AAHLLGRVGL MDSDEWNNIY QALDYPYNAS VGKDGMEQAF ESYLHGVPGK
RAIETNDQGK VVSADDNWKI DERTGEPQAP QPGCNVISTL DIKLQEAVER ALADGVGALK
SEDTQGAAAV VIDVNDGGVL ASASYPTYDL STFLQNYTEL ANDPLNPLFN RATQGVYPPG
STFKMVTAIA GLQEGVITPT DEILDTGRYT YYKDYQPQCW YYRQYGRTHG KENVSEAIRD
SCNIFFYDVG RRLGISLLDE YAQKFGLGEY TGIEVYESKG HVAGPGYTES LGQKWYDGNT
LPAAIGQENN QFTPIQLANY VATLANGGTH YSAHLLKEVK SSDFSQVVYQ YEPEVLNELD
LDPENLEAVT RGMLMVTQPG GSAYSYGFNT LDIQVAAKTG SAQVSSATES NAVFVCFAPY
EDPEIALAIV VEKGGSGSTL SSIAVEILDY YFSSGSGMET VEGENTLLR
//
