ID J3HKT7_9BURK Unreviewed; 639 AA.
AC J3HKT7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=PMI40_03907 {ECO:0000313|EMBL:EJM98655.1};
OS Herbaspirillum sp. YR522.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1144342 {ECO:0000313|EMBL:EJM98655.1, ECO:0000313|Proteomes:UP000007507};
RN [1] {ECO:0000313|EMBL:EJM98655.1, ECO:0000313|Proteomes:UP000007507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR522 {ECO:0000313|EMBL:EJM98655.1,
RC ECO:0000313|Proteomes:UP000007507};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM98655.1}.
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DR EMBL; AKJA01000128; EJM98655.1; -; Genomic_DNA.
DR RefSeq; WP_008118135.1; NZ_AKJA01000128.1.
DR AlphaFoldDB; J3HKT7; -.
DR STRING; 1144342.PMI40_03907; -.
DR PATRIC; fig|1144342.3.peg.3528; -.
DR eggNOG; COG0760; Bacteria.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000007507; 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; 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; PF13624; SurA_N_3; 1.
DR SUPFAM; SSF54534; FKBP-like; 1.
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:EJM98655.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000007507};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 266..369
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 639 AA; 70032 MW; 0B2498CF68CEECB4 CRC64;
MFDFIRTHQR LMQFLLLLFI FPSFAFFGLE GYSRLTDGDN AVAKVAGQTI TKEDWDQAHR
QQLERMRQAY GNQFDSKLFD TPAARRAILE NLIAQRALGA EVVKAKLAVP DSAIQQSILQ
IPGLTKPDGS FDSEQYRVLL AAQGLNQKSY EAGLRREMAL QQLNAAIQTT AFAPRSVAQN
LSALNDQERT VQVLNFRPEA YAAQVKVTDD MLKAYYDKNA RRFEVPEQAS IQYVVLDAAA
VAAQSSVTDA DIAAYYEQNK KLYATEEERR ASHILITVKK DAAAADKAAA KAKAEALVAQ
LRKNPADFAK LAKANSQDPG SAENGGDLGY FGRGAMVKPF EDAAFAQKQG DISNPVESDF
GYHIIQVTGV KPAAVKSLES VKGEIAGEIK KQIAAKRYTE MADQFNNLVY EQGDSLQPVA
DKLQLKIQTA SVTRVPNPAA GAAPYNNGKF LTALFTDDVI KAKHNTEAVQ AAPNTLIAGR
MVDYKPVSKR AFEDVKEQVQ KAVLLEQEQI LATKAGQAKL AELKQNDSSV GFGEPKVVSR
VKSEGWTEQG FNAVMKVDAA KLPAYTGVES PGFGYQVYRV SKVEQPKVVD QARRKTEQEQ
IANALSQQET LAYLAFLREK AKTQLLKGAD SVSADDAAK
//
