ID A0A3L9Z2V3_9FLAO Unreviewed; 701 AA.
AC A0A3L9Z2V3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=BXY75_0906 {ECO:0000313|EMBL:RMA66480.1};
OS Ulvibacter antarcticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Ulvibacter.
OX NCBI_TaxID=442714 {ECO:0000313|EMBL:RMA66480.1, ECO:0000313|Proteomes:UP000271339};
RN [1] {ECO:0000313|EMBL:RMA66480.1, ECO:0000313|Proteomes:UP000271339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23424 {ECO:0000313|EMBL:RMA66480.1,
RC ECO:0000313|Proteomes:UP000271339};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (OCT-2018) 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:RMA66480.1}.
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DR EMBL; REFC01000011; RMA66480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L9Z2V3; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000271339; 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; 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; PF13623; SurA_N_2; 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:RMA66480.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000271339};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 341..448
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 701 AA; 77185 MW; 77C06DB831537D2E CRC64;
MAILNNIRKR GVFLIIIIAL ALFSFILADV IRNGGFSSNK SQTTVAVVNG TDIDRESFMQ
QVENVQRQLG PNGTTSQAMN RVWETELRKV LLEEQYEKLG LSAEKAQIGS AMRQSLAGNP
TFLNEAGQFD EGKMQEYIAS IKTSNPVAYQ QWLDYEKSVE ASVLQDTYYN LIKGGLRSTL
AEGEQEYRFE NDKVNIEYVQ IPYTKIPDGD VTVTDEEIKA YVKEHSSKYE VEAKADIQYV
TFSEEPTLDD VNDAKADIAT LLSPKYQYSD TIQGFAKAVD FEEFVNANSD QPYVDKWQFK
KELPQEAADS IMALKVGQVY GPYKIGNNFN LSRIVETKQL PDSIKSKHIL VRFAGTLRAA
EDITRSKEEA QKLADSLLTV VKRDKSKFDV LAGQFSDDTS NKDKGGDLGY NAPGRMVAAF
DNFTIDNKPG TVGVVETDFG FHVISVEDQK NLQKAVKVAT ITKEIEASEK TMSDVFAQAS
KFELGSQKGD FSTFAKEQNI EVKPVNKIDR MDSNIPGVGN NRSIVNWAFE EDTNVGNVKR
FSVPNGYVIV QVTRKSPKGL MSVAEASTAV TPILRNQKKA KKIRESITGT ELKEIAASQN
VTVQNATALT MAAPTIPGAG AELAVVGAAF SKKAGESTGL IDGKAGVFKV KVLAVNKAPN
LESYTTYANQ LNAKITPTVN NAIFKALKEG ADIEDNRANF F
//
