ID A0A396TW11_9GAMM Unreviewed; 387 AA.
AC A0A396TW11;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Protein HflK {ECO:0000256|RuleBase:RU364113};
GN Name=hflK {ECO:0000313|EMBL:RHW75692.1};
GN ORFNames=D1094_11200 {ECO:0000313|EMBL:RHW75692.1};
OS Colwellia sp. RSH04.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=2305464 {ECO:0000313|EMBL:RHW75692.1, ECO:0000313|Proteomes:UP000266369};
RN [1] {ECO:0000313|Proteomes:UP000266369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSH04 {ECO:0000313|Proteomes:UP000266369};
RA Meng X.;
RL Submitted (SEP-2018) 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}.
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:RHW75692.1}.
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DR EMBL; QXIO01000006; RHW75692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A396TW11; -.
DR OrthoDB; 9779595at2; -.
DR Proteomes; UP000266369; Unassembled WGS sequence.
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:RHW75692.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364113};
KW Protease {ECO:0000313|EMBL:RHW75692.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000266369};
KW Transmembrane {ECO:0000256|RuleBase:RU364113};
KW Transmembrane helix {ECO:0000256|RuleBase:RU364113}.
FT TRANSMEM 62..83
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU364113"
FT DOMAIN 78..238
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 387 AA; 43081 MW; 6CB1A21B8AB9A3E3 CRC64;
MAWNEPGNND KDPWKNKGGK NQGPPDLDEL LNDLGKKVTG IFGGKSSNGG SNSGSGKSFS
SIGLSIILII GLVVYAFSGF YTIKEAEKGI VLRFGKYAGT VDPGINFKWT FIDRVIPVDM
QSTRDLPASG FMLTQDENVV RVDMQIQYRV VDARNYVFSV TNADDSLSQS LDSALRYVVG
HAKMDDILTS GREQIRQSVW QELEKIIERY NLGLIIVDVN FKDARPPNEV KDAFDDAIAA
QEDEIRFIRE AEAYARGIEP RARGRVKRME QEAIAYKEQT LLDAEGEVAR FEKILPEYQA
APDVTRERLY LATMERVYSN TSKVMVDVDG GNNMMYLPLD KIIQQQQPAN RSNNQSYTPA
TTPNSSGNTS PTSSTSGRAD RFNSGRN
//
