ID A0A1Y6HA52_9XANT Unreviewed; 656 AA.
AC A0A1Y6HA52;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN Name=surA {ECO:0000313|EMBL:SMR04254.1};
GN ORFNames=PD5205_02971 {ECO:0000313|EMBL:SMR04254.1};
OS Xanthomonas fragariae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=48664 {ECO:0000313|EMBL:SMR04254.1, ECO:0000313|Proteomes:UP000195953};
RN [1] {ECO:0000313|EMBL:SMR04254.1, ECO:0000313|Proteomes:UP000195953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PD5205 {ECO:0000313|EMBL:SMR04254.1};
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; LT853885; SMR04254.1; -; Genomic_DNA.
DR RefSeq; WP_002806051.1; NZ_ORZZ01000053.1.
DR AlphaFoldDB; A0A1Y6HA52; -.
DR STRING; 48664.BER92_14395; -.
DR GeneID; 61893444; -.
DR KEGG; xfr:BER92_14395; -.
DR eggNOG; COG0760; Bacteria.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000195953; Chromosome 1.
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:SMR04254.1};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 286..387
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 656 AA; 71280 MW; EEC1D0F69C6A02DC CRC64;
MLQKIRDKTS GWIATAILGL LMIPFLFVID NSYLGGIGAN NVAKVQAPPT WWKSAPSWWP
VSLLWQHHEI STQDFRARFE QARMQERQRQ GENFGPRTFE SREDKLQVLD QLVDEQVVRL
GAEDAGIVIG DATVRDYITG IQAFQVDGKF SPDQYRAALA QGTPPRTPAQ FDALVRDSLQ
LSVIPQSVAE SGFATKAEFE RLLRLMGETR DVELAMLPTP VADTAPVSDA QIKQWYDGHT
QDFRQPETVT IEYVELNAAS MPPATAADEA TLRKRYEEEK ARFVEPDQRL ASHILISAGS
DAAAQKAAEA KAATLAAEAK RPGADFATLA KTNSQDPGSK DAGGDLGWVE KGTMVKPFED
ALFSMKAGNV VGPIKSEFGY HVIQLREVKG GQGKSFEQVR DQLAAEQLKA DTDKAFADVS
GKLVDQVYKN PTALEPAAKQ AGLPVQTLGP FSRASASGIA ANPAVLRSAF SEALVQDGTV
SDPITIAPNH SVVLRVTNHT SEQTLPLDKV RDKVIAAIHT DRTQKATAAA ADVLLARVQK
GETLRALAAS EKLQVRPIPG LPRNAPIPTP AANRAIFSAP RPTGGRQSAG KVELDGGRFA
VFVVSKATPG DLKQMPAEQQ TMLRDQLSQI DGNNAAQAYV KEIRKRYKIQ IEEAQL
//
