ID A0A140DWE4_9FIRM Unreviewed; 736 AA.
AC A0A140DWE4;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Cell envelope-related transcriptional attenuator domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AALO17_18370 {ECO:0000313|EMBL:AMK54971.1};
OS Faecalibaculum rodentium.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Faecalibaculum.
OX NCBI_TaxID=1702221 {ECO:0000313|EMBL:AMK54971.1, ECO:0000313|Proteomes:UP000069771};
RN [1] {ECO:0000313|EMBL:AMK54971.1, ECO:0000313|Proteomes:UP000069771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alo17 {ECO:0000313|EMBL:AMK54971.1,
RC ECO:0000313|Proteomes:UP000069771};
RX PubMed=26877770; DOI=10.1186/s13099-016-0087-3;
RA Lim S., Chang D.H., Ahn S., Kim B.C.;
RT "Whole genome sequencing of "Faecalibaculum rodentium" ALO17, isolated from
RT C57BL/6J laboratory mouse feces.";
RL Gut Pathog. 8:3-3(2016).
CC -!- SIMILARITY: Belongs to the LytR/CpsA/Psr (LCP) family.
CC {ECO:0000256|ARBA:ARBA00006068}.
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DR EMBL; CP011391; AMK54971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A140DWE4; -.
DR STRING; 1702221.AALO17_18370; -.
DR KEGG; fro:AALO17_18370; -.
DR PATRIC; fig|1702221.3.peg.1792; -.
DR Proteomes; UP000069771; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 3.40.630.190; LCP protein; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR InterPro; IPR004474; LytR_CpsA_psr.
DR InterPro; IPR015168; SsuA/THI5.
DR NCBIfam; TIGR00350; lytR_cpsA_psr; 1.
DR PANTHER; PTHR33392; POLYISOPRENYL-TEICHOIC ACID--PEPTIDOGLYCAN TEICHOIC ACID TRANSFERASE TAGU; 1.
DR PANTHER; PTHR33392:SF6; POLYISOPRENYL-TEICHOIC ACID--PEPTIDOGLYCAN TEICHOIC ACID TRANSFERASE TAGU; 1.
DR Pfam; PF03816; LytR_cpsA_psr; 1.
DR Pfam; PF09084; NMT1; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000069771};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 106..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 207..299
FT /note="SsuA/THI5-like"
FT /evidence="ECO:0000259|Pfam:PF09084"
FT DOMAIN 340..492
FT /note="Cell envelope-related transcriptional attenuator"
FT /evidence="ECO:0000259|Pfam:PF03816"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..715
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 80725 MW; D696DEAF6B08DEE9 CRC64;
MEQGDTHMKK QKKEREDSRD LSGDLEHNTG AATQAATDET VSPDSERTYT LHTELAGDPA
GTEPEDPFAG TEGASEHFRT KDSRTGGRKT ARTPQKPTEG RKWPDFLLWG LATLLSVLFS
LLLYQMGMLT IQILVCICVI LLLTDLILLI LLLRRTQVRW TTWVWRVFAV IMSACLAFGS
FTIYNTWNAL STITGSNASS ATLKVDLLVP ADSGVSKVTD LVRKKVGYST RADETVVAYA
LNQISTQINE VEYVDYSDYS QLYDDLRDGT IDAMLLPATR YNLLQEQYKD LKKDTKAIAQ
YETTRTLTPT SNSALDISRE PFVVYVAGID AGDDPSIDGR SDVNILVMVD PVNNSMTTVS
VPRDSYVPNP AYNNGSDKLT HLGNDGADNS ILGLEEAFGI EIDYYAKVNF QSLIHIVDAL
GGVEVDVKLD FTEQDENRSF KKDDLITLKK GKQVLNGKEA LAYARHRKTA GYGTTGRENA
QQDIIRAIMK KLTTAEGISR INQLMEAAQK YVATDMPLPA IQKFISQQLK NVQPWTVDSM
TLKGGADATL TTVSMPSLPL SCYLLSPEDI TKVYNAYARM FDDTKMKAFS FDLTKDPQPK
ITYAVEQEVS EYMITSADAD RLSPYSVYYG IDRVDSSSAD RSETRAQENA IDIVVPSYTP
PVYVPEYVDP GPSYTEPVTP APSPSPEPEP APAPEPEPTP TPTPDPTPTP DPTPTPDSGT
SGGSGTDTAA VGEGTD
//
