ID F5YME8_TREPZ Unreviewed; 637 AA.
AC F5YME8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=AMP-binding enzyme family protein {ECO:0000313|EMBL:AEF86159.1};
GN OrderedLocusNames=TREPR_0175 {ECO:0000313|EMBL:AEF86159.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF86159.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF86159.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
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DR EMBL; CP001843; AEF86159.1; -; Genomic_DNA.
DR RefSeq; WP_015706301.1; NC_015578.1.
DR AlphaFoldDB; F5YME8; -.
DR STRING; 545694.TREPR_0175; -.
DR KEGG; tpi:TREPR_0175; -.
DR eggNOG; COG1022; Bacteria.
DR HOGENOM; CLU_000022_45_5_12; -.
DR OrthoDB; 311554at2; -.
DR Proteomes; UP000009223; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43813; ACYL-ACTIVATING ENZYME 16, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR43813:SF1; ACYL-ACTIVATING ENZYME 16, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000009223};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 299..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..461
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 637 AA; 72189 MW; 50E5403FC8A33DB1 CRC64;
MEQTLPLMLR ERVRAIPAVG AQYAKDASGH FQPKTYQQFY DEIRHVAAGL LELGAKRGDH
IGIISDNRQE WLVSDFAVLS IGAADVPRGC DSLEQEIAYI LGFTDCTISF VENQKQITKI
LARREELPLL KTLISYDTVD EKTLEAVKAG GLSVCLYEEL LKMGEKRHSQ NPEEIDAEMN
KGQGEDLATI IFTSGTTGIP KGVMLTHRNF LVQQPSFRLV FETKTGDIWL SVLPVWHVFE
RSIEYVIFYL GNGIAYSKPI SSVLLPDFQN IRPQWMVSVP RVWESIMDWT NRNVKQQGWF
WKNWFNFFVN LGIMYNYFRD LTFGLLPNFH GRIRVLDAII GFFPWVLLCP ARGLAWLLVF
RRVKKRLGGR FRAGISGGGS LPVKVDLFFN AVGLRLQEGY GLTETSPIVA VRRYKAARRN
TVGQVLLDTE CRIVDNKGAI LQPGNNGHLQ VRGGQVMKGY YRKPEETAKV LFDDGWIETG
DIAMMTYDNE VRITGRAKDT IVLRGGENVE PIPIELKIQE SPWVAQCMVV GQDQKYLAAL
IVPVQEAIMG FAEENNIPIV DYDLLLQQPE INELIANDVF QLVSPQAGFK PFERIFKFRL
IPKPFAVGVE LTGKMELIRQ KISANYSREI ANLFKGK
//
