ID A0LTL7_ACIC1 Unreviewed; 638 AA.
AC A0LTL7;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Peptidoglycan synthetase FtsI {ECO:0000313|EMBL:ABK52777.1};
DE EC=2.4.1.129 {ECO:0000313|EMBL:ABK52777.1};
GN OrderedLocusNames=Acel_1004 {ECO:0000313|EMBL:ABK52777.1};
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52777.1, ECO:0000313|Proteomes:UP000008221};
RN [1] {ECO:0000313|EMBL:ABK52777.1, ECO:0000313|Proteomes:UP000008221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B
RC {ECO:0000313|Proteomes:UP000008221};
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
CC -!- SIMILARITY: Belongs to the transpeptidase family.
CC {ECO:0000256|ARBA:ARBA00007171}.
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DR EMBL; CP000481; ABK52777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0LTL7; -.
DR STRING; 351607.Acel_1004; -.
DR KEGG; ace:Acel_1004; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_5_11; -.
DR InParanoid; A0LTL7; -.
DR Proteomes; UP000008221; Chromosome.
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 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 Glycosyltransferase {ECO:0000313|EMBL:ABK52777.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008221};
KW Transferase {ECO:0000313|EMBL:ABK52777.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 66..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 109..258
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 302..608
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 638 AA; 66854 MW; A541B7F612217AC7 CRC64;
MSDLRTGRSP RHRPRPTRTP AQRRQLHLPA TRALRPDPQR TRAVPRRPLR PPVRRGLRLG
EPSRRLHAVL LATVFVVIVF GLRLVEIQGI QGEVYSRQAQ AQYLRSTTLP APRGEIVDRN
GAVLATSVDA RDVVVDPSIA KQSTSPTPQV MAARLAPLLG VPASTLLSRL TGPGRFAYLA
RGVTPAVAAK VLALDLPGVA DEPVLKRSYP NGSLGASVIG FVGIDGNGLG GLEYAYDATL
AGHAGHRTVE TGSDGTVLPD GATTVTPPVP GEGLQLTLDR DIEWEAQQAL AQQVTATGAK
GGTVIVMRPR TGEILAMASV PTFDPAHPQD APPSVLGNPA VSDVFEPGST AKVITMAAAL
DSGILTPTSV IDVPPTLDRA GYTFHDAEPH GEEKLTLTGV LAQSSNIGAI LASERVGTQR
LYQYLRAFGL GEPSGLGFPG ESAGVIGTPQ SWSASQRYTI PFGQGIAVNA MQVADVYATI
ANGGVRVTPT LIKGIIGRDG TLHPAAPPKQ TRVISAAAAR QLEEMLEAVT TDQGTAPAAR
IPGYRVAGKT GTAQRVDPSC ACYRGYTASF VGFAPADDPQ LLVLVVLDDP VNGHFGGAVA
APVFRQVMSF ALQTEKIPPT GTTPPQLPLQ VPSDQPVG
//
