ID A0A0G3AN89_9ACTN Unreviewed; 574 AA.
AC A0A0G3AN89;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Membrane protein {ECO:0000313|EMBL:AKJ13220.1};
GN ORFNames=ABB07_25260 {ECO:0000313|EMBL:AKJ13220.1};
OS Streptomyces incarnatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ13220.1, ECO:0000313|Proteomes:UP000035366};
RN [1] {ECO:0000313|EMBL:AKJ13220.1, ECO:0000313|Proteomes:UP000035366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX PubMed=26159526;
RA Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA Tamura T.;
RT "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT the Nucleoside Antibiotic Sinefungin.";
RL Genome Announc. 3:e00715-e00715(2015).
CC -!- SIMILARITY: Belongs to the LytR/CpsA/Psr (LCP) family.
CC {ECO:0000256|ARBA:ARBA00006068}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP011497; AKJ13220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3AN89; -.
DR STRING; 665007.ABB07_25260; -.
DR PATRIC; fig|665007.5.peg.5369; -.
DR Proteomes; UP000035366; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.2390; -; 1.
DR Gene3D; 3.40.630.190; LCP protein; 1.
DR InterPro; IPR027381; LytR/CpsA/Psr_C.
DR InterPro; IPR004474; LytR_CpsA_psr.
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; PF13399; LytR_C; 1.
DR Pfam; PF03816; LytR_cpsA_psr; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 285..401
FT /note="Cell envelope-related transcriptional attenuator"
FT /evidence="ECO:0000259|Pfam:PF03816"
FT DOMAIN 482..569
FT /note="LytR/CpsA/Psr regulator C-terminal"
FT /evidence="ECO:0000259|Pfam:PF13399"
FT REGION 31..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 574 AA; 60294 MW; 4064DD09530B4EBC CRC64;
MNDRYDAGDA GYGAGPYEIV GYDEYGRPMY QQVPAQPAPQ AQQATYDPYA QQQGYGYDPY
ATGQQPPVTS YDTSRPAPGY DPYGSQAPYD PYGTGTQHPA GYDPYGRAAN SGQQPRVTEQ
TAHIPQQAGP AEGTHAPAQP ARPHDDGERD YHTEQFAFVE EPDGDSEDVI DWLKFTENRT
ERREEARRRA RSRIIALLVV LALVAVGGTG YLWYAGKLPG LSSAGSKPGA ATPVGAQKRD
VIVVHLHNTG KGGTSTALLV DNTTTKQGSM VLLPNSLALS GDDGSTTTLA KSVADDGSSG
TLDQLDTVLG TNIQGTWRLD TPYLQNLVDL VGNIDIDTNT DVPDPDAKKK GAEPLVHKGS
QQTLSGKMAV AYATYRAAGE SEDAQLERFG QVMQGVLRKM SSDPSAATVT VQTLAQILDP
PLTDKDLGTF LAKLADLAKS GAYKTALLPV QADGTLSTRT SDSVVKDILG GTAKSPDAGS
AVRVSVQNAT GVKDDTEKAR VVLINGGFTF LEGGTASGTQ GTSKVVYSDA SHKSDATEVA
KTLGLPAGSV TKGTVSSGAD VSVVLGQDYK PASS
//
