ID   U7US77_9FIRM            Unreviewed;       773 AA.
AC   U7US77;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Penicillin-binding protein, transpeptidase domain protein {ECO:0000313|EMBL:ERT62175.1};
GN   ORFNames=HMPREF1253_1125 {ECO:0000313|EMBL:ERT62175.1};
OS   Peptoniphilus sp. BV3C26.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Peptoniphilus.
OX   NCBI_TaxID=1111134 {ECO:0000313|EMBL:ERT62175.1, ECO:0000313|Proteomes:UP000017105};
RN   [1] {ECO:0000313|EMBL:ERT62175.1, ECO:0000313|Proteomes:UP000017105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BV3C26 {ECO:0000313|EMBL:ERT62175.1,
RC   ECO:0000313|Proteomes:UP000017105};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA   Methe B., Sutton G., Nelson K.E.;
RL   Submitted (SEP-2013) 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:ERT62175.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AWXB01000005; ERT62175.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7US77; -.
DR   STRING; 1111134.HMPREF1253_1125; -.
DR   PATRIC; fig|1111134.3.peg.77; -.
DR   eggNOG; COG0768; Bacteria.
DR   Proteomes; UP000017105; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   CDD; cd06577; PASTA_pknB; 1.
DR   Gene3D; 3.30.10.20; -; 1.
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; IPR005543; PASTA_dom.
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:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR   Pfam; PF03793; PASTA; 2.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SMART; SM00740; PASTA; 2.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
DR   SUPFAM; SSF54184; Penicillin-binding protein 2x (pbp-2x), c-terminal domain; 1.
DR   PROSITE; PS51178; PASTA; 2.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017105};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          612..676
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   DOMAIN          678..736
FT                   /note="PASTA"
FT                   /evidence="ECO:0000259|PROSITE:PS51178"
FT   REGION          738..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..773
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   773 AA;  86419 MW;  7A83DAD76A9AD6CD CRC64;
     MSSNKRIFFT LTVLVFLFIL IAVRLLYIQA FESEELTKAA LRQLTKQESI QSNRGLIYDR
     NKKVMALNVS KSTIYYDSSL IIPRGGKNKG KRESDQQYED RMAKFNIDRK KTLEEDATSL
     ANILNLNRED LLLQISQDKM VRIARDVDRK VALKIRELNN PRISNEDYIK RFYPFGKSAA
     HVLGFLNNEN FGIYGLESYY DDELSGIAGK SIKIKSEQQQ QIPMTKEENY APKNGFNLVS
     SIDVNIQNFA DEAAQKAYNL YEPDKVSIIV QDTKTAQILA MVNLDEYDPN EPRNPINKKQ
     EEEWKGLKDS DKVDLWAENW KNFSVESQYE PGSTFKLITA AAAIEEATTN PSRVYTCPGV
     LTDMKGVKIS CTSKNRGPRT FLEAMEESCN ITLVKVGREL GPERFLKYIR AFGFGDKTGI
     DLKGEVNGTI PKDPKHISKV SISTMSYGHG IAVTPIQLIN AVSAIGNGGF LNEPRIIKEV
     VDNDGNIIEK FKTNTLRRVI SQETSKTLKD IMAKVVEEGT GKKAQVPGYK IGGKTGTAYI
     ASANGYEDEY NSSFIGLAPA MDPQITVLVV INRPKGDFYG ATVAAPIAQE VMAKSLEYLK
     VPKTEKVDEN ALKEDIEVPD VTNRLVIDAG KILVDAGLRF NTPNKNTKDS SVVISQNPKA
     GSIVKNGTII DVELNDPDEE KIMPLMTGMK DQQAESILKA LNIEYNIVGN GSIVSQKPLP
     GTRLTEESKI LLKCDNLTNY DENKSEDENS FEEKNSHKEN GKNNNENNNK KNR
//