ID A0A1I3AQ38_9PROT Unreviewed; 624 AA.
AC A0A1I3AQ38;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=SAMN05216299_11868 {ECO:0000313|EMBL:SFH52082.1};
OS Nitrosospira sp. Nsp14.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=1855333 {ECO:0000313|EMBL:SFH52082.1, ECO:0000313|Proteomes:UP000198772};
RN [1] {ECO:0000313|EMBL:SFH52082.1, ECO:0000313|Proteomes:UP000198772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nsp14 {ECO:0000313|EMBL:SFH52082.1,
RC ECO:0000313|Proteomes:UP000198772};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOPV01000018; SFH52082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3AQ38; -.
DR STRING; 1855333.SAMN05216299_11868; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000198772; 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; IPR023058; PPIase_PpiC_CS.
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; PS01096; PPIC_PPIASE_1; 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:SFH52082.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000198772};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 263..366
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 624 AA; 69639 MW; 2146DF8C5B41635F CRC64;
MFDFVHRKRR IVQIIMGLAV LPFLFWGVES YRSNEGEDYV ALAAGERIQR QEFDQAMRNQ
QESMRATMGE NFNDAMLDRP EVRSAVLEGL IQQRLLKHEA SGAGLAVLDP QLVEMIQNIS
AFQEDGKFSK QRYEELLRGQ GMTPRTFEAR VRQELMRQQL IAPYSENGFV SATVAQKLMR
LSEEQREISL VQILPAAFLA RVKPDETAIK AYYDSHQAEF QLPEQAQVEY AVLSLEKLAE
RTPVSTEEAM KYFEEHKSEF GQTEERRASH ILLSAPASAP DAERQAARAK AEQLLVQVKK
APQRFAELAK QHSQDPGSAA TGGDLGYFGR NMMVKAFEDA VFQMKPDEVS DIVETDFGFH
VIKLTAIKDA KSIDFNEVRG QVEEQLKKEK AAKLFAEMAD GFSNLVYEQS DSLQPAAEKF
GLSLQRSGWI GKDAGEPPYL TGRLLQGIFS DDAVKGKRNT EAVEVAPNTL VAARVLDHRP
TRMQTIAELK DKISALVAQQ EARALAGKEG KEKLAQLHAG KGSDISWGAV QRVSRKEPQG
LDNDTLRAIF KADAAALPSY SGVENSQGVF TLIRVNRVIQ PDVPDPATRK AFAKQLQQVL
TQEELSSYLA GVRTRYDVSL GNVN
//
