ID A0A1Y6IPH2_9VIBR Unreviewed; 617 AA.
AC A0A1Y6IPH2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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 Name=ppiD {ECO:0000313|EMBL:SMR99555.1};
GN ORFNames=VIM7927_00781 {ECO:0000313|EMBL:SMR99555.1};
OS Vibrio mangrovi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=474394 {ECO:0000313|EMBL:SMR99555.1, ECO:0000313|Proteomes:UP000196125};
RN [1] {ECO:0000313|EMBL:SMR99555.1, ECO:0000313|Proteomes:UP000196125}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7927 {ECO:0000313|EMBL:SMR99555.1,
RC ECO:0000313|Proteomes:UP000196125};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) 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; FXXI01000001; SMR99555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6IPH2; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000196125; 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; 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; 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:SMR99555.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..359
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 617 AA; 68732 MW; C0B643E7243F2021 CRC64;
MMDRLREGAN SIAIKIILGL IVLSFVFAGV GRYLVSGSNN AVAEVGSTKI SRTEFEQAYQ
NERNRMQSQL GDYFSNLLAD PSYVASFRRS VLDKMVNDVL LEQHAESLGL RISDEQVRQA
IVDMPQFQSD GKFDQEIYQS ALRRAGFTPD SFAGFLRSDL LRNQLLTAVQ SSDFTLDGEV
NAQAALFSQK REIRSITLAT DDYAKKVQLS DDDLNAYYKS HEEDFMRPEQ FKISYIELSA
DQLKQSVEVT DDEAEKYYQD HADQYSSKAQ RKVSHILVND EKQADTLLQQ LKSGADFAKL
AKENSQDPGS ASDGGSLDWF EKGVMDPAFE EAAFALKNVG DLSGVVKSNF GYHIIKLDAV
KSATVKPFSE VKDDVIASIR DERALDHFYQ LQSELEKVAF ESPDSLDEAA KTIQAKINTT
DFVSLNDVPE VLRSAPVQKA LGNPEVKNEG LNSSVIEVAP EDVVVVRIEE SRPESLLPFD
TVKDQVVGTL SKVKAEQQTQ EIASEALTAL EQGDQSVLEK HQLKFGKLTL IDRRSPLAQA
VFAMKKPQDS QAVYGQTKDS QGNVVLVELA KIESTTDDQL AEQLGVQMQR LNRQQDLAGL
LNILREQTDI EYYLATQ
//
