ID A0A1H0Z0W2_9GAMM Unreviewed; 658 AA.
AC A0A1H0Z0W2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=SAMN05216569_0101 {ECO:0000313|EMBL:SDQ21004.1};
OS Pseudoxanthomonas sp. CF125.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1855303 {ECO:0000313|EMBL:SDQ21004.1, ECO:0000313|Proteomes:UP000199049};
RN [1] {ECO:0000313|EMBL:SDQ21004.1, ECO:0000313|Proteomes:UP000199049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF125 {ECO:0000313|EMBL:SDQ21004.1,
RC ECO:0000313|Proteomes:UP000199049};
RA de Groot N.N.;
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; FNLD01000001; SDQ21004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0Z0W2; -.
DR STRING; 1855303.SAMN05216569_0101; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000199049; 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; 2.
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:SDQ21004.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000199049};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 285..389
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 658 AA; 71195 MW; 9E6849F710AE23FA CRC64;
MLQTLRDKTS GWIATIVLGL LIIPFAFVGV NEYMGGGTDN AVAKVEAPPT WWKSAPTWWP
VSMFWQHEEV TQEEFRARFE QARQQQREAM GENFDAREFE TQENKLLVLD QLIDRKVMQL
NAKRSGIAVS DDAVRKTITE AFQVGGKYDQ ASYAAFLSGR GMTAAKFESE QRDNLQLALI
PQGIAESGFV TGKEMDRLIK LLGETRDVTI AALKAPEIGA DTAAVTDAQI KAWYEAHPAD
YKQGESVSLE YVDVDAATLS PTTAPVDEAA LRKRYEQEKS RFMSAEQRLA SHILIMVPAD
ANAAAQKAAE QKAAALAAQA KQPGADFAAL AKANSQDDGS KNNGGELPWV ARDGTMTKPF
EDAMFSMQPG EISGPIKTEF GYHVLQLREI KPGQGKSFEE VRDVLAREQA DSEGERAYND
LAGRVVNEVL KNPTSLAPAA KAVGLPVQRI GPFSRATASG IAANPAVLRA AFSDSLVQDG
TVSDPIEIGP KHAVFIRVLQ HTPEQAQPIA QVRDAVIAAI RTDRAAKAAE KAADAILARI
AKGETLQAIA AADKLQTGEL PGIPRGAPMP SPEINAAIFA TQKPAAGKAS VGKARMEDGN
YVVFVVNKVT EGDLTKITPE QRMQLQQQVA QMGAAGDVAS YVGALRKQYK ITRREDKL
//
