ID H0E8K3_9ACTN Unreviewed; 732 AA.
AC H0E8K3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Cell division protein FtsI [Peptidoglycan synthetase] {ECO:0000313|EMBL:EHN10003.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:EHN10003.1};
GN ORFNames=PAI11_31640 {ECO:0000313|EMBL:EHN10003.1};
OS Patulibacter medicamentivorans.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Patulibacteraceae; Patulibacter.
OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN10003.1, ECO:0000313|Proteomes:UP000005143};
RN [1] {ECO:0000313|EMBL:EHN10003.1, ECO:0000313|Proteomes:UP000005143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I11 {ECO:0000313|EMBL:EHN10003.1,
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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:EHN10003.1}.
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DR EMBL; AGUD01000244; EHN10003.1; -; Genomic_DNA.
DR AlphaFoldDB; H0E8K3; -.
DR PATRIC; fig|1097667.3.peg.3137; -.
DR Proteomes; UP000005143; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 3.40.710.10; 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:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 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:EHN10003.1};
KW Cell division {ECO:0000313|EMBL:EHN10003.1};
KW Glycosyltransferase {ECO:0000313|EMBL:EHN10003.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000005143};
KW Transferase {ECO:0000313|EMBL:EHN10003.1}.
FT DOMAIN 44..299
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 345..705
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 116..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..131
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 79885 MW; 5589E4B15217BAFA CRC64;
MAAFGIVAFG VFAVLFLRLW FMQILQGDDY LAKATENPAR VVRVAAGRGG IIDRNGNVLV
KNEVANVVSL KSDAVPEADR ARVSNWGHDI GVHEVKVERR ATQLLDQSVS RAVARAAGRS
RKARRKARIP TVRQKKDADR QAARELAADK PDDLTLKDAS PLLVAKLERV SPILKTSPQR
LYQRVVAGIV KVPAGNVPLK RKVSLPVKNY LLERQADFPG LTVTKEYIRE YPGKQLAAQI
FGAVGQISES QLKQERYRGL VAGQQIGQGG LEQEYDSVLR GKDGEQRVQV DAQNRPTGKV
TDVKPKQGRR LRLTLDLGLE RVGQFGMQQA IGRKIDDKTK KRAGGAYVAL DPRDGSVLAM
GSYPSIDPNV FNRDITAQQF KQLTSARNGA PLINRAIQGL YPTGSTFKPI TAAAGLTSGV
IGLQTRQGTG SCIKLGDQDQ EFCNAGSADH GDTNLVQALT VSSDTYFYLV GWNLFPLPNQ
PLQTWAHLFG FGRTSHIDLP GEDAGTVPSS EWRKQRDKDE RACRRQRKVA SCGLVFKIGD
TYKRGDNVNL SVGQGDLLAT PLQLAVAYSG LYDPTDRVTG ELRFPVPRLG DQVESSQGVL
EQKLPRPKPR VVKFPVEYKT AILTGLWNVT REGDGTAAGV FAGWNQSQYP VMGKTGTAER
CPKTKPCSDQ SWFAAMVPDP TRPIVVVATV ENGGFGTETA APIVCRMLRS FYQQSPSQAA
CDAKQTGSNP NE
//
