ID H0E556_9ACTN Unreviewed; 565 AA.
AC H0E556;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Cell division protein FtsI [Peptidoglycan synthetase] {ECO:0000313|EMBL:EHN11186.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:EHN11186.1};
GN ORFNames=PAI11_19430 {ECO:0000313|EMBL:EHN11186.1};
OS Patulibacter medicamentivorans.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Patulibacteraceae; Patulibacter.
OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN11186.1, ECO:0000313|Proteomes:UP000005143};
RN [1] {ECO:0000313|EMBL:EHN11186.1, ECO:0000313|Proteomes:UP000005143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I11 {ECO:0000313|EMBL:EHN11186.1,
RC ECO:0000313|Proteomes:UP000005143};
RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT strain I11.";
RL Biodegradation 24:615-630(2013).
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:EHN11186.1}.
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DR EMBL; AGUD01000137; EHN11186.1; -; Genomic_DNA.
DR RefSeq; WP_007573979.1; NZ_AGUD01000137.1.
DR AlphaFoldDB; H0E556; -.
DR PATRIC; fig|1097667.3.peg.1926; -.
DR OrthoDB; 9789078at2; -.
DR Proteomes; UP000005143; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 Cell cycle {ECO:0000313|EMBL:EHN11186.1};
KW Cell division {ECO:0000313|EMBL:EHN11186.1};
KW Glycosyltransferase {ECO:0000313|EMBL:EHN11186.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000005143};
KW Transferase {ECO:0000313|EMBL:EHN11186.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 50..211
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 252..553
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 565 AA; 60230 MW; 7C4019173A58AC2A CRC64;
MYADRRLRVL FSIAMFLLVV AGGRSVWFAL AKADTLTAAA RGQQNTPREI LAARGEIQDR
YGAPLAVSEP ADDVAVSPRV VTEQLTLKPA QRPQQLADLV ASELDLPEDE VLKKLTANAG
YVRLARSVPD RKVQALRDRA LKMNVSLAAL TFEPRNRRIY PGGALAGQLL GAYGDDDKAL
AGLEIGYDKS LRGTNGKELE TRSQTGSPLR TVTERKMVPG KNVSLTLDTR IQAVAEEALQ
QLGQTYRPKK ATAIVMRPDG EILSMANWPR VDPNQPGESP EWAKANSATG FTYEPGSTFK
AVAVGGALQD HTVTPTSQFT VPYSIQVADR VIKDSHGHGT EVMTPGQILA QSSNVGTIQI
GQKLGSKRFD GWMRKLGFGS TTGLGWPGEE QGLLPKLENY SGSTMGNLPI GQGQLVTPMQ
IANLYATIAN GGMLRHPSLV RTIGGQRVAR PAGKRVLRPD VAQQLRGMLA GVFEAGGTAS
AVKVPGYQLA GKTGTSNVFD TKLGEYVENR NVASIAGFAP ANNPKLVIVV VADEPAGGGY
GATVAGPAFG DIAKFALQYL KIPPK
//