ID A0A136Q576_9FIRM Unreviewed; 719 AA.
AC A0A136Q576;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Penicillin-binding protein, transpeptidase domain protein {ECO:0000313|EMBL:KXK65838.1};
GN ORFNames=HMPREF3293_01331 {ECO:0000313|EMBL:KXK65838.1};
OS Christensenella minuta.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Christensenellaceae;
OC Christensenella.
OX NCBI_TaxID=626937 {ECO:0000313|EMBL:KXK65838.1, ECO:0000313|Proteomes:UP000070366};
RN [1] {ECO:0000313|EMBL:KXK65838.1, ECO:0000313|Proteomes:UP000070366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22607 {ECO:0000313|EMBL:KXK65838.1,
RC ECO:0000313|Proteomes:UP000070366};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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:KXK65838.1}.
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DR EMBL; LSZW01000055; KXK65838.1; -; Genomic_DNA.
DR RefSeq; WP_066521041.1; NZ_MAIR01000004.1.
DR AlphaFoldDB; A0A136Q576; -.
DR STRING; 626937.HMPREF3293_01331; -.
DR KEGG; cmiu:B1H56_12440; -.
DR PATRIC; fig|626937.4.peg.1313; -.
DR OrthoDB; 9766847at2; -.
DR Proteomes; UP000070366; 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:UP000070366};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..719
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039661222"
FT DOMAIN 40..148
FT /note="NTF2-like N-terminal transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF05223"
FT DOMAIN 155..322
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 363..695
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 441..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 78713 MW; B220FB70BA7D7782 CRC64;
MKKKLLIYIL VPLLLLVFTG AAFTGCSTLT DSADSVGGAF VNKLVARDYS GAFDYVYVLT
ADVGTRDEFV ARFTNIYDAL EVSDVKLVSR SVEPVSDNEY ELKYTLALTS RLLGVLTYDY
SADIVAGPQG YTVLYTPSLI LPMLEEGDRV RSTTQEGARG EIFSADGAVL AKNDYADSVY
IDLEKGPDIE EVKAFLTANF SVDAETIQKK YDNAVEKGYP LEVLLSYPKG TITDEQKEAV
AGINGLGFDD SRFSPVRYYP LKDDAAHIIG YLGSPSDEQL AANEDLTEYS TVGKSGLEMQ
YEEVLRGSDG RIIYIEDEKG SLKQVLFEDE KTDGQNIELS IDSKTQERAY TLMASNLVDG
QSGAVIVMDY STGAVEAMVS YPSFDNNLFN FPLDEATWNY YNGDEDHPLI NRAIQSAYMP
GSSFKPFSSL PAIEGGLLDA DSVPPITKKP PHSEGNEESG SHSWTPDIEG WHSGAIYSKT
VAESPYNYEM AMKSSDNIFF AYYALQAGVD PFESYMEKIG IGEAPQFELP VTASSMLSQS
EDEVDWLDWL ARTGYGTGEL VITPLQLACM YTAIENGGTM VNPHIVNRTF TIEGEDETET
TVEETSVSAF KEGTMSQKAI DIIKPALKRV MVDGTGYEAR LGDRDVLGKT GTAQVGANNS
REVNWIIALN QEDGKLYMVV VETDTDEGTK PKTSILRGLA DESAYSRMLS GVSSSGEEE
//