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Database: UniProt
Entry: A0A144NSA8_9GAMM
LinkDB: A0A144NSA8_9GAMM
Original site: A0A144NSA8_9GAMM 
ID   A0A144NSA8_9GAMM        Unreviewed;       624 AA.
AC   A0A144NSA8;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE   AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN   ORFNames=A3K91_0861 {ECO:0000313|EMBL:AMT96480.1};
OS   Psychrobacter alimentarius.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=261164 {ECO:0000313|EMBL:AMT96480.1, ECO:0000313|Proteomes:UP000076104};
RN   [1] {ECO:0000313|EMBL:AMT96480.1, ECO:0000313|Proteomes:UP000076104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 27889 {ECO:0000313|EMBL:AMT96480.1,
RC   ECO:0000313|Proteomes:UP000076104};
RA   Lee J., Kim O.-S.;
RT   "Genome sequencing of Psychrobacter alimentarius PAMC 27889.";
RL   Submitted (MAR-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; CP014945; AMT96480.1; -; Genomic_DNA.
DR   RefSeq; WP_062844163.1; NZ_CP014945.1.
DR   AlphaFoldDB; A0A144NSA8; -.
DR   STRING; 261164.A3K91_0861; -.
DR   KEGG; pali:A3K91_0861; -.
DR   PATRIC; fig|261164.3.peg.913; -.
DR   OrthoDB; 9812372at2; -.
DR   Proteomes; UP000076104; Chromosome.
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:AMT96480.1}; 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          262..357
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   624 AA;  69094 MW;  C1C9A0C02ACE6B61 CRC64;
     MDKLRDFLKS WPGRILLILC LSPLALLGVE SYFGGGVDPN QIAQVGDASV GLSEYQTAVN
     NRRTEILEQV DDASLLNEDV LHEQVLKGLV DRTLLEQQAG KLGMTVSDDT INRLLREEEI
     FKDAEGNFSN DQFANFLRQR GMTKNQLFAE FRNQLSLDQL NASIVGTAVY PMKAVSQLID
     LQLESRNIWL YRFKWQDYAE QVKVSKSDIQ SYYDANKNTL KSAAMVDLAY LQLTPQSIQV
     NDVTKEDLQQ QYDAYKQSQA INDERQISQI LLTGDDAKAR ADKIKARLNK GESFAALAKA
     ESDDPSGETG GDIGRFNPTV FGNDAEAVEK ALEGLSVGGV TAPVKTSFGY QIFTVTEDNG
     SKMPTLESMR DELTAKAKEY KRQEMYADKV TAINDLAADG FSIEDIAQQE NVTLKRIKDY
     TKENNQSVLS QPAVIKQAFD EFTIQDQAVT AGIEVGNGNV WVQPSNYRPT KTLTLAAATP
     KITQILRQQK ATALAVKQAK TLAAGIKTPA DIGKQPVRLQ SLGSVNRQTT RLTEKERGLA
     FSQQAADNGV VAVASETETG ATLLVGDRIK TEQQSPLSEM QRAQTATIIR DNLGQDQLQD
     YLDYLRLVYK VEINEANMKN AQGR
//
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