ID A4BW22_9FLAO Unreviewed; 707 AA.
AC A4BW22;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=PI23P_01677 {ECO:0000313|EMBL:EAR13163.1};
OS Polaribacter irgensii 23-P.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=313594 {ECO:0000313|EMBL:EAR13163.1, ECO:0000313|Proteomes:UP000003053};
RN [1] {ECO:0000313|EMBL:EAR13163.1, ECO:0000313|Proteomes:UP000003053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=23-P {ECO:0000313|EMBL:EAR13163.1,
RC ECO:0000313|Proteomes:UP000003053};
RA Murray A., Staley J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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:EAR13163.1}.
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DR EMBL; AAOG01000001; EAR13163.1; -; Genomic_DNA.
DR RefSeq; WP_004568956.1; NZ_CH724148.1.
DR AlphaFoldDB; A4BW22; -.
DR STRING; 313594.PI23P_01677; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_023843_0_1_10; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000003053; 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 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; PF13623; SurA_N_2; 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:EAR13163.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000003053};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 344..451
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 707 AA; 77539 MW; FC4FE08ED9E14BB9 CRC64;
MAILSKIRER SMFLIIIIGL ALFAFVLDPS TLGDFFSSSK VNEVGQVNGE AISRQEFAEA
VDQYKQNSRS EVSEMQAANA VWDNILRKKI YKNQLEDAGI SVGEQDVWSE ILKVPSVQDN
PQFQNEAGLF DELKFKQFLA DTKENNQSLW SAWSNYMGQI KENTETNTYN SLVTAGLGAS
LKEGEMEYVI ENTKLSGDFV YVSYASIADS LVSIKRSEVA AYIKANENEF KAVSTRDISY
VKFDIKATAE DEEAIKQKVG SLIGDASDRN NEVIVGFKNA TDDKVFLVDN GSDLNLDEDY
KFNASISQAV ANDIFSGNEG DVFGPYKDQG YFKISKIRAV TKMPDSVRAS HILIPFLGSQ
RGTAEVSRTK AQAEELADSI LRVVKRSDSK FASLAKSLSS DTGSAAKGGD LDWFNYARMT
PAFRDYAFTN SKGAVGVVET PFGYHVIRID DTKNTQKVLK LSTYASKIIP SEATENDFFQ
KAEQFALAVS KTTDYTALAK ENNYNLRAAV GLEVLDENVP GLGNERQIVS WAFKGDSKIG
SFNRFDLTGS YVVAVVTSKT EKGLMSVEKA LNTVRPILLN EKKAALISAN LKGSSLAAIA
AANNTTVRNA KDVNLKTASL VGVGVEPKIV GAMYGAELNK VYNAIVGNRG VFSFALNKKE
APTALPNYEV NRKRISASRK AMTFKIYEAI KSASEVEDNR ASMYGSN
//
