ID A0A2T0R8N1_9ACTN Unreviewed; 635 AA.
AC A0A2T0R8N1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Peptidoglycan synthetase FtsI {ECO:0000313|EMBL:PRY17531.1};
GN ORFNames=CLV37_102494 {ECO:0000313|EMBL:PRY17531.1};
OS Kineococcus rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Kineococcus.
OX NCBI_TaxID=559628 {ECO:0000313|EMBL:PRY17531.1, ECO:0000313|Proteomes:UP000238083};
RN [1] {ECO:0000313|EMBL:PRY17531.1, ECO:0000313|Proteomes:UP000238083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19711 {ECO:0000313|EMBL:PRY17531.1,
RC ECO:0000313|Proteomes:UP000238083};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PRY17531.1}.
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DR EMBL; PVZF01000002; PRY17531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0R8N1; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000238083; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 66..234
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 280..591
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 635 AA; 66572 MW; FC5845B069D2937F CRC64;
MSRRRPRPEA TDPGRHPRPD MRMRVYTVGV LGGLGILGGR LVQLQGADAN ALAGRALKQR
TSQTTLYAKR GDIVDDEGVV LATSVERRDV IADPKAVAGF NLRANGEPYK AGRGTGPAGA
AALLAPILGI DEQTLTAKLT GDNHYAKVAV GITPELWQQV SDVGVAGITS VRQTQRIYPT
GAASSTLVGI LGTAETDDDG NVVDKPLSGL EYADQHLLQG RNGLMRYERS LGGQEIPLGN
RETTEPVDGT SLHLTIDSDL QWKAQTAIAA KVVETGARSG TVVIMDKEQR LLALASAPSI
DPANLTGMTN AQLQNTALTE AFEPGSTAKV VTLAAALEEG VDTADSRFTV PGELKRFDKT
FHDSHPHGDE KLTLAGVLAQ SSNIGTILAG EKLDPDLKKV SQILHGYQQK FGFGSRTTLE
FPGETAGIVG DPAKYSGTQR YTVMFGQGIS VNAVQAASVF ATIANDGVRT EPTLISGTSD
PNGNYRAEPA GESTRVVSAA TAKTLRDMMQ AVVSEEGTAA AAAIPGYLVA GKTGTAERYD
SDLGRYSGYT ASFIGMAPAD DPELVVAVIL QDPKTNYYGG SAAGPVFKEV MSYALVQRGV
APSTRPPADL PLTWGGDQDA EQEIATGAVG DTAGQ
//
