ID A0A177HIV1_9ACTN Unreviewed; 317 AA.
AC A0A177HIV1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Modulator of FtsH protease HflK {ECO:0000313|EMBL:OAH10560.1};
GN Name=hflK_1 {ECO:0000313|EMBL:OAH10560.1};
GN ORFNames=STSP_61210 {ECO:0000313|EMBL:OAH10560.1};
OS Streptomyces jeddahensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1716141 {ECO:0000313|EMBL:OAH10560.1, ECO:0000313|Proteomes:UP000077381};
RN [1] {ECO:0000313|EMBL:OAH10560.1, ECO:0000313|Proteomes:UP000077381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25(2015) {ECO:0000313|Proteomes:UP000077381};
RA Poehlein A., Roettig A., Hiessl S., Hauschild P., Schauer J., Madkour M.H.,
RA Al-Ansari A.M., Almakishah N.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Streptomyces sp. G25.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family.
CC {ECO:0000256|ARBA:ARBA00008164}.
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:OAH10560.1}.
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DR EMBL; LOHS01000135; OAH10560.1; -; Genomic_DNA.
DR RefSeq; WP_067284148.1; NZ_LOHS01000135.1.
DR AlphaFoldDB; A0A177HIV1; -.
DR STRING; 1716141.STSP_61210; -.
DR PATRIC; fig|1716141.3.peg.6435; -.
DR OrthoDB; 9809197at2; -.
DR Proteomes; UP000077381; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd08829; SPFH_paraslipin; 1.
DR Gene3D; 3.30.479.30; Band 7 domain; 1.
DR InterPro; IPR001107; Band_7.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR018080; Band_7/stomatin-like_CS.
DR InterPro; IPR001972; Stomatin_HflK_fam.
DR PANTHER; PTHR43327; STOMATIN-LIKE PROTEIN 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43327:SF10; STOMATIN-LIKE PROTEIN 2, MITOCHONDRIAL; 1.
DR Pfam; PF01145; Band_7; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
DR PROSITE; PS01270; BAND_7; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:OAH10560.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Protease {ECO:0000313|EMBL:OAH10560.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077381};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 21..179
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 290..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 317 AA; 34581 MW; 92B0BB73DCA57B4D CRC64;
MEPIIIVLII LVVLVFIALI KTIQVIPQAS AAIVERFGRY TRTLNAGLNI VVPFIDSIRN
RIDLREQVVP FPPQPVITQD NLVVNIDTVI YYQVTDARAA TYEVASYIQA IEQLTVTTLR
NIIGGMDLER TLTSREEINA ALRGVLDEAT GKWGIRVNRV ELKAIEPPTS IQDSMEKQMR
ADRDKRAAIL TAEGIRQSQI LTAEGEKQSA ILRAEGEAKA AALRAEGEAQ AVRTVFEAIH
AGDPDQKLLS YQYLQMLPKI AEGDANKLWI VPSEIGDALK GLSGAIGNFG PATGGSGNQS
GNSNGSGTER REQPRID
//