ID A0A1G1NHU0_9BACT Unreviewed; 532 AA.
AC A0A1G1NHU0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=A3B78_02220 {ECO:0000313|EMBL:OGX29181.1};
OS Omnitrophica WOR_2 bacterium RIFCSPHIGHO2_02_FULL_67_20.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801860 {ECO:0000313|EMBL:OGX29181.1, ECO:0000313|Proteomes:UP000180285};
RN [1] {ECO:0000313|EMBL:OGX29181.1, ECO:0000313|Proteomes:UP000180285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGX29181.1}.
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DR EMBL; MHGT01000016; OGX29181.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1NHU0; -.
DR STRING; 1801860.A3B78_02220; -.
DR Proteomes; UP000180285; 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; -; 2.
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; 2.
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};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 380..479
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 264..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 59781 MW; 3539358624F5860B CRC64;
MFRRLFLSQA ARRRTSWLIA AVLILPFIFF FHASIRTPAK GEGGTAGTLF GKSVPWEVFQ
REQRWIRFKL QTVAGQMPFD VLEPMVNQAA WERLMLLEEA KRRGLRVDDL ELASAIQGFP
DFQKDGRFVA ERYHLFLRAS GLTPQLFEEW LRGDLLMEKL RDAVRSEVTV TDEDVRAAFV
RAHEQLAASV IVMEPGSFID GAAKTVTEDD VRARYEARPD EVRRPEQVAF EYAGISRESL
AGAVSLTDED LQGHYEARQD EFLAADGTPK PFEEAREPVR QSLTSERVRK QLTERGLDLE
EDLEAKRPFD EIATARGLTK QTAGPLNPRS PAPGGPDPAL LQAVAELDEG NMSEVVRTTA
GVYIARVTRR IPATVPPLEE VRDAIRERLI RERARGSARQ AAEVVLAKLQ ARIAYGVRFE
EAVLADGVSV TRARFGRTQP IDPLGYERAV NETAFAAPLG QLTPVLETAR GFAVLRPEEY
LPPDEAAFAQ EEPALRSETL TRRQEERFGE WLQEVRGRAK LTSFVDGIAD ER
//
