ID V9TS43_9PROT Unreviewed; 622 AA.
AC V9TS43;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Parvulin-like PPIase {ECO:0000256|ARBA:ARBA00018370};
DE AltName: Full=Peptidyl-prolyl cis-trans isomerase plp {ECO:0000256|ARBA:ARBA00030642};
DE AltName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
DE AltName: Full=Rotamase plp {ECO:0000256|ARBA:ARBA00031484};
GN ORFNames=P856_492 {ECO:0000313|EMBL:AHC73709.1};
OS Candidatus Endolissoclinum faulkneri L5.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Endolissoclinum.
OX NCBI_TaxID=1401328 {ECO:0000313|EMBL:AHC73709.1, ECO:0000313|Proteomes:UP000018700};
RN [1] {ECO:0000313|EMBL:AHC73709.1, ECO:0000313|Proteomes:UP000018700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=faulkneri L5 {ECO:0000313|Proteomes:UP000018700};
RX PubMed=24324632;
RA Kwan J.C., Schmidt E.W.;
RT "Bacterial endosymbiosis in a chordate host: long-term co-evolution and
RT conservation of secondary metabolism.";
RL PLoS ONE 8:E80822-E80822(2013).
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; CP006745; AHC73709.1; -; Genomic_DNA.
DR RefSeq; WP_025300589.1; NZ_CP006745.1.
DR AlphaFoldDB; V9TS43; -.
DR STRING; 1401328.P856_492; -.
DR KEGG; efk:P856_492; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_023843_1_0_5; -.
DR OrthoDB; 9768393at2; -.
DR Proteomes; UP000018700; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
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; PF13145; Rotamase_2; 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.
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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000018700};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 239..361
FT /note="PpiC"
FT /evidence="ECO:0000259|Pfam:PF13145"
SQ SEQUENCE 622 AA; 69908 MW; 62395CC15B7170D8 CRC64;
MVRSFFIKIL FIVLIVSFLV WSTGDAIFSS FNNRREAISV NGEVLVTAID AKKEFERLYQ
QFRYPITVKH AIQIGLLEET MRKLSEQSLI LTAANSLGLS VSNTEVVRMI HKQFCDSMGR
FDREAYRSFL SSNGWEEVDF IRRINHDILR DQLITSIINS NSSIVPEVFV KALHEYRNER
RIAAAVRIDA ASLPYPKLPD YSLISAYYEK HKNEYETPEY RKVSWIALSV DNLAKNIKIS
NDELIDIFEE RKDLFTTKDS RTIDQAIFQT KEDARIAYNR IQAGESFSAV VEEMTGKKAG
NINVIKVTRN EVLDDVAAEA VFNISKPGTV SKPVKSELGW TLFNILDVEV GVSANFEEMR
DDLKHDLLLE RAYEQLFKYS SAMEDALAGG LSIEEISQLM KIPLHQISFL SRAGLPSGNM
QDNDLPGDPF LDVALKTENG AYSGVTKTNN GDAFFVLQVN GVTPSQIPEL KDVRERIVLD
WMAEQRLETS KKIADTIVSE VNNGTSLLHS TAKHGLQVER LPAINRNGDS LPSVWPNAIV
DALFEQKVGE AKAVSSKEGT AIISLIKVIK DRSDVAFVNK HIQHEFISAS AQDLFELLLA
ELKSNNNVVV NSSNVYQLLS IN
//
