ID A0A1M5C9P1_9BACT Unreviewed; 707 AA.
AC A0A1M5C9P1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN05444274_10614 {ECO:0000313|EMBL:SHF51463.1};
OS Mariniphaga anaerophila.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Mariniphaga.
OX NCBI_TaxID=1484053 {ECO:0000313|EMBL:SHF51463.1, ECO:0000313|Proteomes:UP000184164};
RN [1] {ECO:0000313|EMBL:SHF51463.1, ECO:0000313|Proteomes:UP000184164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26910 {ECO:0000313|EMBL:SHF51463.1,
RC ECO:0000313|Proteomes:UP000184164};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQUM01000006; SHF51463.1; -; Genomic_DNA.
DR RefSeq; WP_073002303.1; NZ_FQUM01000006.1.
DR AlphaFoldDB; A0A1M5C9P1; -.
DR STRING; 1484053.SAMN05444274_10614; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000184164; 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 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; PF13623; SurA_N_2; 1.
DR SUPFAM; SSF54534; FKBP-like; 2.
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:SHF51463.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000184164};
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 347..445
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 707 AA; 78760 MW; 9A069BFF46C650AD CRC64;
MATLQTIRTK AGLLVAIVIG ISLAAFILGD MFQGGSSILQ GNRMEVGEVN GESIQYPQFQ
QEVEKLGDIY RMNTSQNQLD ENTWVQVREQ TWQTMIRDIV MNDVYKKIGI TVSSDELFDM
LQGTNLHPIV QQLFRNPNTG QVDRGAVVQF LKNLETGVAP EQRHYWLYLE NQIVDERIQS
KYNSLVGKGL YVTSQEASNS LAGRNKEVSF DYVALNHTSV ADSQVVVTEK DLKDYYNKNQ
DTYKQEKLRQ IEYITFPVEP SEQDFKDTEK WINDVVSDFA SATDNAAFVN SNSDVDFDDT
WYKQSDLPED IATWVFENDA KINDIFGPYF EDNAYKLAKL HASEMLPDSV EARHILLQVN
TQQELIAQQA LADSLKTAIE NGSDFSKLAM EFSADQGSAI QGGELGWFGR GQMVKPFEEA
AFNNKVKEVS VVTSQFGIHI IQTTARGQLS RQVQIAYLVR NVTPSTQTYQ SVYAKASEFA
GKNVTKEDFD AAATEQKINK RSASLRETDR QVAALENSRQ LVRAAFSSKV GSIVEDQQGS
TIFDFGDNFV IATLVSASEE GVASFESVKA RVELAVLKEK KLQFLAEKAK KAMEGKTDLE
AIASELGSTV KNAANINLTS IQIPGIGMEP KVVGTATNMS PDQISQPVAG KNGVYIIKVI
TVNEGDNQDT EGERARLAQS LTFRAASQAY NVHREKAEIE DERSKFY
//
