ID A0A084INW0_SALHC Unreviewed; 631 AA.
AC A0A084INW0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=C41B8_05813 {ECO:0000313|EMBL:KEZ78394.1};
OS Salinisphaera hydrothermalis (strain C41B8).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Salinisphaera.
OX NCBI_TaxID=1304275 {ECO:0000313|EMBL:KEZ78394.1, ECO:0000313|Proteomes:UP000028302};
RN [1] {ECO:0000313|EMBL:KEZ78394.1, ECO:0000313|Proteomes:UP000028302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C41B8 {ECO:0000313|EMBL:KEZ78394.1,
RC ECO:0000313|Proteomes:UP000028302};
RA Li C., Lai Q., Shao Z.;
RT "Salinisphaera hydrothermalis C41B8 Genome Sequencing.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004382}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004382}; Periplasmic side
CC {ECO:0000256|ARBA:ARBA00004382}.
CC -!- SIMILARITY: Belongs to the PpiD chaperone family.
CC {ECO:0000256|ARBA:ARBA00038408}.
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:KEZ78394.1}.
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DR EMBL; APNK01000005; KEZ78394.1; -; Genomic_DNA.
DR RefSeq; WP_037335325.1; NZ_APNK01000005.1.
DR AlphaFoldDB; A0A084INW0; -.
DR STRING; 1304275.C41B8_05813; -.
DR eggNOG; COG0760; Bacteria.
DR Proteomes; UP000028302; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.4030.10; Porin chaperone SurA, peptide-binding domain; 1.
DR InterPro; IPR046357; PPIase_dom_sf.
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.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW ECO:0000313|EMBL:KEZ78394.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028302};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 245..356
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 631 AA; 68975 MW; 407B90A0DF7006A7 CRC64;
MLQKIRDGAS GPLAYIVVAV IAVVFGVWGI GSYFTPSSDP VVASAGGTNI THSELQQAFN
QRYQRLRQMM GDHFDSSMFP QDEIRKNVLD NLIDQAVMTQ YAQDQGYRVT DANLLAEIRS
NPQFQDNGKF SPQRYKALLR QAGIEPSQYE ARLRQGMLGD QVRQVVVGSA FAAPPEVDVA
YRRAHEQRKV DVLTFDSSAY ADQVKIDDAA IKTYYDKHPK QFMRAPRVKL AYVSLDADQL
SPKAPDQATL KQLYKAHKNE FGTPAKRSAD EVRIPIGQDD AKARQAVQKA VAAAKQGQSL
KQVASSIDGA QFRQIDSQPQ SALPDAVGSA LFGLKQGALS TPVRGDKAWY VLRTTAITPA
KTPAFDDPVV QARLKAMATQ QERAKAFRQK SDKLDDLAYQ APNGLKTISD KLGLKIQHTG
WISQNGGGSG LGQYSAVRKA AFSDAVLKDQ LNSKVLDLGN QRHVVLRVTD HQKAQRKPLA
EVRDTIRSRL IARESQQRAK KAAQQAMAKA RQGQSLEQIA QAGKGAKLTQ AGFVGRDDSK
LDPNALGAAF DMPMAQKKSA PTQYRVVSTD NGQAALVAVL GSRVQSGGGQ GPKRAQIAQQ
QSGYNASLEY SALDRYLRKQ ADVKIHKSAM N
//
