ID A0A2Z5R1A3_9MICC Unreviewed; 615 AA.
AC A0A2Z5R1A3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=DipZ protein {ECO:0000313|EMBL:BAV88458.1};
GN ORFNames=RA11412_2159 {ECO:0000313|EMBL:BAV88458.1};
OS Rothia aeria.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=172042 {ECO:0000313|EMBL:BAV88458.1, ECO:0000313|Proteomes:UP000250241};
RN [1] {ECO:0000313|EMBL:BAV88458.1, ECO:0000313|Proteomes:UP000250241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11412 {ECO:0000313|EMBL:BAV88458.1,
RC ECO:0000313|Proteomes:UP000250241};
RA Nambu T.;
RT "Genome sequence of Rothia aeria strain JCM11412.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP017895; BAV88458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z5R1A3; -.
DR KEGG; raj:RA11412_2159; -.
DR Proteomes; UP000250241; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd03012; TlpA_like_DipZ_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR041017; Thioredoxin_10.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42852:SF13; PROTEIN DIPZ; 1.
DR PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF02683; DsbD; 1.
DR Pfam; PF17991; Thioredoxin_10; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000250241};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 301..451
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 596..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 66232 MW; 908C0E95117E794D CRC64;
MLLSLIILGI LGGLITGISP CILPILPVIL VTGGADSART ASVDNGQTDT VKDSANNVQA
LFSRRSAVLT NTTSAPTQRT ASRWRPYQVV GGLVLSFSLF TLLGSVILAA LHLPQDTLRI
LGITFLIIVG LSMFIPPLER LLEKPFAKFS QLGAKRSTTR GGFLMGLALG LVYVPCAGPV
LAAITLAGAT GNIGIETVAL TLSFALGTAI PLLIFALAGR SIAERVKTFR THQRGVRTAS
GILLIALSIG LIFNVPAQLQ RAIPNYTEGI EQAISQGTQN NIISSSAGGA ISTCRPDEEK
LQDCGSAPEL TGGTGNFNTK NQPTLTNLRG KVTLVDFWAY SCINCQRTAP HLNELYAKYR
DYGLEIVGVH TPEYAFEHEA KNVQAGIENL GIKYPVVQDN DYAIWRAYSN RYWPAHYLID
SEGKLRAVHY GEGGHKVTEA QVRELLKAAN PQVQLPDPIH KDDAQEQTQN THDARTPETY
LGAKRAMYFA GHGNYSSGTQ TFKPADRLDI DHFDLNGTWA ITPNVLSLKE ATALCGLTIV
PTGCRLLPVA AAPLKCGATA QRKRSTLTAL LMLTTLCVAM SKAAGLLNSK SRRECSCTRS
PSHKSTPRNL RWAHP
//
