ID A0A1T4KW35_9ACTN Unreviewed; 651 AA.
AC A0A1T4KW35;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Peptidoglycan synthetase FtsI {ECO:0000313|EMBL:SJZ46645.1};
GN ORFNames=SAMN02745673_00571 {ECO:0000313|EMBL:SJZ46645.1};
OS Marinactinospora thermotolerans DSM 45154.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Marinactinospora.
OX NCBI_TaxID=1122192 {ECO:0000313|EMBL:SJZ46645.1, ECO:0000313|Proteomes:UP000190637};
RN [1] {ECO:0000313|EMBL:SJZ46645.1, ECO:0000313|Proteomes:UP000190637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45154 {ECO:0000313|EMBL:SJZ46645.1,
RC ECO:0000313|Proteomes:UP000190637};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; FUWS01000001; SJZ46645.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4KW35; -.
DR STRING; 1122192.SAMN02745673_00571; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000190637; 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:UP000190637};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 87..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 130..277
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 322..628
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 651 AA; 69922 MW; 0DCC2FCF98D0877B CRC64;
MSTPRDPRPR NPRRRGTPDR TVKGTSPREN GGQGRPRGSV DPARTGTAAK GGRPRPRGKA
VPSRRPPRGP VPPLRRRFRR SDPGPRIRIA LALMGVVLLV FAGRLVQIQG IEAASYASAA
AELRLSETEI PTTRGSITDA DGRPFAMSVE VRTVFVDPYD VKADERDTIV TELSRRFDLP
EEEVARKVDS DDSRYQVIAR EVPLEEWKEL DELDLQGVAA ETAYKRVYPE ETGAANLVGF
VGTDGHGLEG LESVLEDTLA GDPGSRQVEL GTGGTEIPMA NGVAKEPVPG HDVRLTLDQD
VQWRAQQALA QRAGELGADS GSVIVMRPTG EIVAMANYPT YDPDAIEEST PEQRANGALS
AAFEPGSTNK VITAAAALEE DVVTPDTVYT VPDSIRRHGE TFRDSHNHPT QRMTLNGIMA
TSSNVGTIKV AEDVGAEGLY EYLGKFGFGE PSGLGLPGEN SGILTAPDEW WGTQLASISF
GHGISVNAVQ MASVYATVAN DGVRVEPTVI AGSTDENGEF RPAPEPAKER VISEETAREL
RLMLEAVTGE HGTAQDARIP GYRVAGKTGT ANRVDPDTGS YDTGGYTSTF VGMAPADDPE
LIVQVVLHNP KEQYYGGEAA APVFTDVMSF ALKTLQIPPT ATEQPNIRLF E
//
