ID A0A240AQH9_SERFI Unreviewed; 416 AA.
AC A0A240AQH9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN Name=hflK {ECO:0000313|EMBL:SNV85116.1};
GN ORFNames=SAMEA4384070_00453 {ECO:0000313|EMBL:SNV85116.1};
OS Serratia ficaria.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=61651 {ECO:0000313|EMBL:SNV85116.1, ECO:0000313|Proteomes:UP000215134};
RN [1] {ECO:0000313|EMBL:SNV85116.1, ECO:0000313|Proteomes:UP000215134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12148 {ECO:0000313|EMBL:SNV85116.1,
RC ECO:0000313|Proteomes:UP000215134};
RG Pathogen Informatics;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: HflC and HflK could encode or regulate a protease.
CC {ECO:0000256|RuleBase:RU364113}.
CC -!- SUBUNIT: HflC and HflK may interact to form a multimeric complex.
CC {ECO:0000256|RuleBase:RU364113}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU364113}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflK subfamily.
CC {ECO:0000256|ARBA:ARBA00006971, ECO:0000256|RuleBase:RU364113}.
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DR EMBL; LT906479; SNV85116.1; -; Genomic_DNA.
DR RefSeq; WP_061799876.1; NZ_QTUE01000001.1.
DR AlphaFoldDB; A0A240AQH9; -.
DR STRING; 1411141.GCA_001590885_04221; -.
DR GeneID; 75025644; -.
DR KEGG; sfj:SAMEA4384070_0453; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000215134; Chromosome 1.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03404; SPFH_HflK; 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; IPR010201; HflK.
DR InterPro; IPR020980; Membrane_HflK_N.
DR InterPro; IPR001972; Stomatin_HflK_fam.
DR NCBIfam; TIGR01933; hflK; 1.
DR PANTHER; PTHR43327:SF2; MODULATOR OF FTSH PROTEASE HFLK; 1.
DR PANTHER; PTHR43327; STOMATIN-LIKE PROTEIN 2, MITOCHONDRIAL; 1.
DR Pfam; PF01145; Band_7; 1.
DR Pfam; PF12221; HflK_N; 1.
DR PRINTS; PR00721; STOMATIN.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:SNV85116.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Protease {ECO:0000313|EMBL:SNV85116.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215134};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 94..254
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 45199 MW; 65F4C47BA78DCD94 CRC64;
MAWNQPGNNG QDRDPWGSSN NNGGNSGGNN KGGRDQGPPD LDDIFRKLSK KLSGLGGGKG
SSGNSGGTGT SGPGFSGRII GIAAVAVVVI WAASGFYTIK EAERGVVTRF GKFSHLVQPG
LNWKPTFIDE VRPVNVESVR ELAASGVMLT SDENVVRVEM NVQYRVTNPE AYLFSVVNAD
DSLSQATDSA LRGVIGKYSM DRILTEGRTV VRNDTQRMLE ETIRPYNMGI TLLDVNFQAA
RPPEEVKASF DDAIAARENE QQYIREAEAY ANEVQPRANG QAQRLLEDSK AYKDRTILEA
QGEVASFAKL LPEYKSAPEI TRERLYIETM QKVLSHTRKV LVSDKGNNLM MLPLDQMLRG
QANAADGGNK DSSLIRLNPA PSANGGSSSQ RTGNGSVMDQ RRANAQRDDT TRVGRE
//
