ID A0A0S8JU19_9BACT Unreviewed; 672 AA.
AC A0A0S8JU19;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=AMJ85_00385 {ECO:0000313|EMBL:KPL13096.1};
OS candidate division BRC1 bacterium SM23_51.
OC Bacteria; Candidatus Sumerlaeota.
OX NCBI_TaxID=1703761 {ECO:0000313|EMBL:KPL13096.1, ECO:0000313|Proteomes:UP000051549};
RN [1] {ECO:0000313|EMBL:KPL13096.1, ECO:0000313|Proteomes:UP000051549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_51 {ECO:0000313|EMBL:KPL13096.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPL13096.1}.
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DR EMBL; LJUL01000003; KPL13096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8JU19; -.
DR Proteomes; UP000051549; 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 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; PF13616; Rotamase_3; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 275..389
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 672 AA; 77411 MW; BE9AFE8F28DD57C9 CRC64;
MLKQLRSRRV MKRIMLGTLI LIIPPFVFYF GWQSTSGRGA EARRDLARVK DRWWGLRWRP
ITAGEWQLAR DSLEREYARI FQSQGLDFSP DQMRKEIGSY EIAREAIDSY YLQRLARREG
LEVTRGEIRA LLEELFPVQP AESFRSYLER VGQSEAQFIR DLVYRQTLSK AEGYIFSRAK
TSLFELWHEY LISQEKIQIR YVRIPSMDFE KEVQPTTDSL SQFYQDHAED YRIGDRAEFR
YVAILRSDVE RETEPTTESV RAFYEKHKGD QLRRKRSARV RHILIEAAPD APTTAVQAAE
QTVRQIAERV KAGEDFAQLA DQFSEDSANI VDPDDPTKKR GGLLPMEITE GMPSRFGEEF
TSEALSLALD EVSSPVRSAF GFHLIRADSV TTAGIVPFDE VREQARRLLR LDLVDAEFRK
RGEALRELFA ERSYSTLDSF AEAAGLQIGR TGLVDLEAGF LPEIGLIRDD LELIREFSEG
EFTEGVLKNS GAYYVLELHR KVPSHIPPFV EVADDVRDDY ITSQAAYLAH EVASELFRQA
ENLEDLEQAA QQRGYEVTQS DPFTRDRADT VLPALDPRFA YTSVRYKVGT IYLTTQGDPE
LPTACIVWYF EKREPPTLAQ FRKDLPALRA EYQLQIQQAL VQEWLRDMRR RIRAEINPVF
EAAAQESEGE SG
//
