ID A0A1F8M4W8_9CHLR Unreviewed; 627 AA.
AC A0A1F8M4W8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Penicillin-binding protein 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2Z71_02765 {ECO:0000313|EMBL:OGN93703.1};
OS Chloroflexi bacterium RBG_13_50_21.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797623 {ECO:0000313|EMBL:OGN93703.1, ECO:0000313|Proteomes:UP000177581};
RN [1] {ECO:0000313|EMBL:OGN93703.1, ECO:0000313|Proteomes:UP000177581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGN93703.1}.
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DR EMBL; MGMQ01000142; OGN93703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8M4W8; -.
DR STRING; 1797623.A2Z71_02765; -.
DR Proteomes; UP000177581; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR Gene3D; 3.30.450.330; -; 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; 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; 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 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..225
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 297..606
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 68879 MW; F594C0CD6DEBDB74 CRC64;
MAEQVVSAGR IRRRQPTNKV SESIHSVNDK AGQTLTGWRF NLLGILFLFA GVMIVIQLVR
LQFSPERNEF VSQGDQYSRT LHIFYPPRGD IYDRWGRLLA GSTLVYEVGV QVDDVENVDT
VAFALSKVLM AHPEYDYPGY YDEIYAVIIK AQKSGTAYIQ LADFVTPEEL SILQEWARNY
SNLPEVDYGK VGRPSLSGLV YRPRLQRYYP ENELGANVLG FVNREGTGMF GVEAEFNDLL
AGVPQSIWMT LDPYQVTEIP QLKPGVDLVL TIDREIQATA EEVLDNALED SGADGGVLLV
MDPNTGEMLA IATTPRLNPN EFWNYASVFK DSTPYNRAIS QDYEPGSVFK VLTMAAGLDD
GAVTMETEFV DTGSIQIGGI YIHNWDWGAW GPQNMEGCMA HSLNVCLTWV ATQLGAGPFY
QYMQNFGFGQ VTGIDLAAEA SGRLKIPGDA DWYEADLGTN AFGQGVAVTP IQMVMAISSV
ANGRGEMMIP HVMRSMVRDG FQYTPTPQII GHPISTDTAQ TLTDLLASSL EGESSDALVE
GYRVAGKTGT AEIATPTGYT SDATNASFVG WGPVKDPKFL VYVWLEKPTS SPWGSVVAAP
VFRDMVERLV VLMDIPPDDV IQGLANH
//
