ID A0A1N7MS87_9RHOB Unreviewed; 615 AA.
AC A0A1N7MS87;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peptidyl-prolyl cis-trans isomerase D {ECO:0000313|EMBL:SIS88811.1};
GN ORFNames=SAMN05421759_105128 {ECO:0000313|EMBL:SIS88811.1};
OS Roseivivax lentus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=633194 {ECO:0000313|EMBL:SIS88811.1, ECO:0000313|Proteomes:UP000186684};
RN [1] {ECO:0000313|EMBL:SIS88811.1, ECO:0000313|Proteomes:UP000186684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29430 {ECO:0000313|EMBL:SIS88811.1,
RC ECO:0000313|Proteomes:UP000186684};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PpiD chaperone family.
CC {ECO:0000256|ARBA:ARBA00038408}.
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; FTOQ01000005; SIS88811.1; -; Genomic_DNA.
DR RefSeq; WP_076448105.1; NZ_FTOQ01000005.1.
DR AlphaFoldDB; A0A1N7MS87; -.
DR STRING; 633194.SAMN05421759_105128; -.
DR OrthoDB; 9768393at2; -.
DR Proteomes; UP000186684; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR PANTHER; PTHR47529; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE D; 1.
DR PANTHER; PTHR47529:SF1; PERIPLASMIC CHAPERONE PPID; 1.
DR Pfam; PF13145; Rotamase_2; 1.
DR Pfam; PF13624; SurA_N_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF109998; Triger factor/SurA peptide-binding domain-like; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Isomerase {ECO:0000313|EMBL:SIS88811.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 245..362
FT /note="PpiC"
FT /evidence="ECO:0000259|Pfam:PF13145"
SQ SEQUENCE 615 AA; 64868 MW; 8EA015F16FD0F353 CRC64;
MALKAGRISK FFLWILMGLL LVGLAGFGAV NLSGTARSVA AVGDKEVSVD AYARAVQQEL
RALQAQRGAA VSFSEARQAG LDTQVLSQLV LTRALDYEAA RLGISVEDSA VAAELAQVGA
FQGPNGQFSR DAYAFALDNA GMTEGEFEAD LRDETARTVF QGGVFSGLTM PAAYTDAIIA
YAGETRDLTY AVLTAADLEA GIDSPTEDDL RAFYDENIDR YTIPETKRVT YAWVTPDMIL
DSLEVPEETL REAYEEQSSQ FNMPERRLVE RLVFSGAAAA EEAAARIASG EISFEALVAE
RGLSLSDTDL GAVSRDDLGD AAEAVFAAET GSVAGPAPTG LGPALFRVNA ELSAVETSFE
EAVPMLRDTL VLDRARRVLA AQAESFDNEL AGGATLEELA QTTDMTLGEI AWTRDSDSGI
AAYPAFNRAV RAAEEGDYPE VVELGDGGMF ALRVDGIDPP APAPFETVEA EVAAAWEEAR
ITEALLVQAE AHAEALSQGA SFADRNLPAT TIAGVERTTP QDRLPRGAIA DAFDAEAGTA
IAVAGSDRVA VIRVDAVTPA DTESEAARSL AEQLSQQAEA ALADDLFRAL AADIQTRAGV
TVNQDALNAV NSSLQ
//
