ID A0A1H0DNW2_9ACTN Unreviewed; 687 AA.
AC A0A1H0DNW2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Peptidoglycan synthetase FtsI {ECO:0000313|EMBL:SDN71753.1};
GN ORFNames=SAMN05216259_105292 {ECO:0000313|EMBL:SDN71753.1};
OS Actinacidiphila guanduensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310781 {ECO:0000313|EMBL:SDN71753.1, ECO:0000313|Proteomes:UP000199341};
RN [1] {ECO:0000313|EMBL:SDN71753.1, ECO:0000313|Proteomes:UP000199341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2022 {ECO:0000313|EMBL:SDN71753.1,
RC ECO:0000313|Proteomes:UP000199341};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; FNIE01000005; SDN71753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0DNW2; -.
DR STRING; 310781.SAMN05216259_105292; -.
DR Proteomes; UP000199341; 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 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199341};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 82..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 125..292
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 336..651
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 71818 MW; E73F74B28FA9CE88 CRC64;
MTPRDESGAP DGADRRRPAR PRTTAGGAAG GAGRAGGARG PVPGRQRGPA RGPARPVRPA
ARGRVPRAAG RVMRLGAARP RLRLVGAVLT VVMAVFVVRL LQVQAVDASA YAAKAEVNRW
VTHEVTADRG TITDRDGVDL ATTVDAFDIT ADPLMFTPAQ AKVNDAPQQA AQLLAPIVGG
DPTAIAKQLA TPHSRYQIIA HQQSPQAWNQ IQDLKSALAA KAAAGEGADV LAGIFSVPHS
KRVYPAGDLA AGVIGFVNSD GRGAGGLESM LDKELAGRNG KIRYAQSDGR QVPTAGSQEQ
PAVPGTDIQL TLDRDIQWAA QNAITQQVQK SRADRGYVIV QDPRTGQVLA MADAPGYDPN
DLAHADPQAL GNAAMQDAYE PGSVSKLMSM AAIIDTGTAT PTTRVTVPGT LPRADRLFHD
DVDHGTWYLT LNGVLAKSSN IGTIEATGQL GRTQAQANQV LYSYLRKFGI GQPTGIGFPG
ETPGILAEPQ DWNASQQYTI PFGQGLSVNA LQATSVYSTI ANGGVRVEPS LIRGTTGPDG
RFVPADPPKK TRVVSARTAK TLSEMLESVV GSEQGTGINA RIAGYRVAGK TGTANRVDPK
TGRYKGYTSS FLGFAPADDP RVTVSCVIQN PTRGSYFGGD ICGPVFKQVM QFALKSLGVP
PTGKPAPNLP VTFDPGQPAT TPGKQVG
//
