ID A0A519W600_9SPHI Unreviewed; 312 AA.
AC A0A519W600;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Protein HflC {ECO:0000256|PIRNR:PIRNR005651};
GN Name=hflC {ECO:0000313|EMBL:RZK67250.1};
GN ORFNames=EOO85_25785 {ECO:0000313|EMBL:RZK67250.1};
OS Pedobacter sp.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1411316 {ECO:0000313|EMBL:RZK67250.1, ECO:0000313|Proteomes:UP000315466};
RN [1] {ECO:0000313|EMBL:RZK67250.1, ECO:0000313|Proteomes:UP000315466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PMG_053 {ECO:0000313|EMBL:RZK67250.1};
RX PubMed=30498029; DOI=.1073/pnas.1812668115;
RA Crombie A.T., Larke-Mejia N.L., Emery H., Dawson R., Pratscher J.,
RA Murphy G.P., McGenity T.J., Murrell J.C.;
RT "Poplar phyllosphere harbors disparate isoprene-degrading bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:13081-13086(2018).
CC -!- FUNCTION: HflC and HflK could regulate a protease.
CC {ECO:0000256|PIRNR:PIRNR005651}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflC subfamily.
CC {ECO:0000256|ARBA:ARBA00007862, ECO:0000256|PIRNR:PIRNR005651}.
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:RZK67250.1}.
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DR EMBL; SEDA01001440; RZK67250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A519W600; -.
DR Proteomes; UP000315466; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03405; SPFH_HflC; 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; IPR010200; HflC.
DR NCBIfam; TIGR01932; hflC; 1.
DR PANTHER; PTHR42911; MODULATOR OF FTSH PROTEASE HFLC; 1.
DR PANTHER; PTHR42911:SF1; MODULATOR OF FTSH PROTEASE HFLC; 1.
DR Pfam; PF01145; Band_7; 1.
DR PIRSF; PIRSF005651; HflC; 1.
DR SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:RZK67250.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protease {ECO:0000313|EMBL:RZK67250.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000315466};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 21..207
FT /note="Band 7"
FT /evidence="ECO:0000259|SMART:SM00244"
SQ SEQUENCE 312 AA; 35639 MW; 2C42937A1E6EA6A0 CRC64;
MKIKQILTII AALFALIFLI ASTFTVSEYE QVVVTQFGRP IGNAITKPGI NFKMPFIQTA
NVFEKRFMEW VGDPNQLPTK DKKFIFVETY ARWQITDPLQ FFKRLTNERG AQSRLDDILD
GETRNVVAKN NIEELVRSSN RKPELDSIGE VLGDSLAIVF VGRDKMQNMI LASANKQAVE
LGIKILDFRF KRINYVQEVQ TQVYERMKSE RFRIADKFRS EGQGEASRIN GEKDRELKTI
QSGAFKRAEE IKGKADANAA SIYASAYNQS EQSKNLYGFL KSMETLDKSF SEKTSVILST
NSDIYKYLKK AE
//
