ID   A0A1H1NSC5_9FLAO        Unreviewed;       706 AA.
AC   A0A1H1NSC5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE   AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN   ORFNames=SAMN04488552_1841 {ECO:0000313|EMBL:SDS01884.1};
OS   Christiangramia echinicola.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Christiangramia.
OX   NCBI_TaxID=279359 {ECO:0000313|EMBL:SDS01884.1, ECO:0000313|Proteomes:UP000198858};
RN   [1] {ECO:0000313|EMBL:SDS01884.1, ECO:0000313|Proteomes:UP000198858}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mar_2010_102 {ECO:0000313|EMBL:SDS01884.1,
RC   ECO:0000313|Proteomes:UP000198858};
RA   Varghese N., Submissions S.;
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; LT629745; SDS01884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1NSC5; -.
DR   STRING; 1250231.SAMN04488552_1841; -.
DR   Proteomes; UP000198858; Chromosome I.
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; PF13623; SurA_N_2; 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:SDS01884.1}; 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          347..453
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   706 AA;  77623 MW;  4C6F53D8383F1E20 CRC64;
     MAVLNKIRQR SVFLIIIIAL ALFSFVLADV IRNGGLSSQN SQNVIATVNG DEISREEFAR
     EVEAFERNMG RNVSTTQAVN RIWDQKLREV ILNEQVDELG IRAGEGQITN LVRSQMAGNP
     NFTNEAGMFD ENRLREYVAN LKETSPEAYA QWQQFTSNLA KTAKLNTYYN MVSAGVGATL
     LEGEQAYRLQ NDNINMKFVQ VPYSSIPDSE VEVTKSDIKS YIDNHSSRFE TDASRSLQYV
     IFTESASGDD KSEAKEAISS LRDQRVEYNA AIGANDTLAG FDSTDDYGDF ISNNSDLPFE
     NRFKFRNDFS GDNAEAIFNL NEGETFGPYE ENGYWKLSKV VETKNIPDSV KASHILVAYE
     GTQLGAGSAR NKEEAKQLAD SIANVARADK EKFADLASEY SADTSNKEQA GDLGYFVPGM
     MIPAFENYVF DNSTGDIGVV ETPLGYHVIS IEDQTEAAKA VKVATIAREI QASEKTMNDL
     FNEVTKFEIS ASEGDFSEVA KKENYEVKTV KDIKALEENI PGAGAQRRVI QWAFGDEASV
     GDVRRFDTNN GYIVAQLTSK KDKGLMSVEE ASSTVTPILK KEKKAEVIKS RLKGSTLQEI
     ASNQGVSVQT ADAVNLSSPT LAGAGEEPEV VGAIFSLEAG KVSEPIAGEK GVYVGELVSK
     FEAPAMDSYK GFAQQESAAR RAQAGSRVFE ALKKKAEIED NRSRFY
//