ID X7ELZ4_9RHOB Unreviewed; 392 AA.
AC X7ELZ4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Protease {ECO:0000313|EMBL:ETX16188.1};
GN ORFNames=OCH239_08505 {ECO:0000313|EMBL:ETX16188.1};
OS Roseivivax halodurans JCM 10272.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=1449350 {ECO:0000313|EMBL:ETX16188.1, ECO:0000313|Proteomes:UP000022447};
RN [1] {ECO:0000313|EMBL:ETX16188.1, ECO:0000313|Proteomes:UP000022447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10272 {ECO:0000313|EMBL:ETX16188.1,
RC ECO:0000313|Proteomes:UP000022447};
RA Lai Q., Li G., Shao Z.;
RT "Roseivivax halodurans JCM 10272 Genome Sequencing.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. HflC subfamily.
CC {ECO:0000256|ARBA:ARBA00007862}.
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:ETX16188.1}.
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DR EMBL; JALZ01000002; ETX16188.1; -; Genomic_DNA.
DR RefSeq; WP_037258801.1; NZ_JALZ01000002.1.
DR AlphaFoldDB; X7ELZ4; -.
DR STRING; 1449350.OCH239_08505; -.
DR PATRIC; fig|1449350.3.peg.748; -.
DR eggNOG; COG0330; Bacteria.
DR OrthoDB; 9812991at2; -.
DR Proteomes; UP000022447; 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:0022900; P:electron transport chain; IEA:InterPro.
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; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR010200; HflC.
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 SMART; SM00244; PHB; 1.
DR SUPFAM; SSF117892; Band 7/SPFH domain; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ETX16188.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000313|EMBL:ETX16188.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000022447};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..29
FT /note="Cytochrome oxidase subunit II transmembrane region
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50999"
FT REGION 309..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..392
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 392 AA; 43664 MW; 650ECF26AAB2FF03 CRC64;
MRWTALPLVA IIAVIVVLWS SLFIVDEREK ALVLQFGQIK QVREEPGIGF KVPLIQEVVT
YDDRILSLDT ETIEVTPADD RRLIVDAFAR YRIADVVQFR QAVGIGGVQL AEDRLSGILN
AQIREVLGAD QVTSDRILSQ DRRDLAIRIR EQARQSAESL GLEIVDVRLK QTNLPQQNLE
ATFARMRAER EREAADEIAR GNEAAQRVRA AADRTVVETT SNAGREAEII RGEADAERNR
VYAEAFGDNP EFFSFYRSLT ALERSLQRDN STLVLSPDSE FVGPLFEAIR AEGLEGVEIS
DTDVERLREL APQSEISPDL PDSAREEIER STQEAEREIE ERRNQERPQG AEPGPGAAED
AAPDENATDD GAETPSETED TPSEEEDAPV SN
//
