ID A0A1E8F9E9_9ALTE Unreviewed; 628 AA.
AC A0A1E8F9E9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=BFC17_05120 {ECO:0000313|EMBL:OFI32542.1};
OS Alteromonas lipolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1856405 {ECO:0000313|EMBL:OFI32542.1, ECO:0000313|Proteomes:UP000176037};
RN [1] {ECO:0000313|EMBL:OFI32542.1, ECO:0000313|Proteomes:UP000176037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JW12 {ECO:0000313|EMBL:OFI32542.1,
RC ECO:0000313|Proteomes:UP000176037};
RA Wu Y.-H., Cheng H., Xu X.-W.;
RT "Alteromonas lipolytica, a new species isolated from sea water.";
RL Submitted (SEP-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OFI32542.1}.
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DR EMBL; MJIC01000016; OFI32542.1; -; Genomic_DNA.
DR RefSeq; WP_070178070.1; NZ_MJIC01000016.1.
DR AlphaFoldDB; A0A1E8F9E9; -.
DR STRING; 1856405.BFC17_05120; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000176037; 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:OFI32542.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000176037};
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..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 268..366
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 628 AA; 68955 MW; AE102373A104CE11 CRC64;
MLERIREGSQ GPWAMAIIAL IVLSFVFAGV SSYVNSSGVT AAAEVNGEPI SQQDVERAYQ
AQRARLESQF GEGISALFSD ENYLRDFRLN VLERLIADTL VQQKADDMGL RVSDKQIREA
ITAMPEFQTD GRFDNERYQM LLRQNGFQPS DFRDYMRQQM TREQLVRALQ ASDFSLPAEV
NTAHVLQGQT RNADYLIVDS APFAKKVEIT DAEVEAFYQE NLSRFDTQEK VNLAYVSLAV
EDLKGEVSVN DEEIEQAYRD NIALYKTDEE RRVSHILVEF GDDKAAAKSQ AEALLADLGQ
GADFAALAKE NSADTFSAEN GGDLDFITAG LMDPAFDEAA FAIADVGDTS GIVETEFGFH
IIKLTDIKPV EVTPLADVRD EIEAQLLTDK ATDEFYALQS DMANLAFEVP DTLEDVAGAV
NGTIRETGLV TAAAVPVPLN VPAVTSKMFD PDFIEEGLNS DVIELSNDNV VVVRVVGHEP
QRTQSLDEVR TQILAQLRAQ KAQEAAFNWA TTVVEQLNAG ETPALVVDDM SLEWESKEAI
TRNSSELPRN LVDLLFTLGT DAPDNIDIAK LGSGDAGVVR LTAINAPAAL SDEEQTRLKQ
QVMATYSQAN YQSFVDSLRA AADVTINL
//
