ID I8T4Y4_9GAMM Unreviewed; 644 AA.
AC I8T4Y4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN ORFNames=WQQ_39980 {ECO:0000313|EMBL:EIT68803.1};
OS Hydrocarboniphaga effusa AP103.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Hydrocarboniphaga.
OX NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT68803.1, ECO:0000313|Proteomes:UP000003704};
RN [1] {ECO:0000313|EMBL:EIT68803.1, ECO:0000313|Proteomes:UP000003704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP103 {ECO:0000313|EMBL:EIT68803.1,
RC ECO:0000313|Proteomes:UP000003704};
RX PubMed=22933753; DOI=10.1128/JB.01017-12;
RA Chang H.K., Zylstra G.J., Chae J.C.;
RT "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT AP103T (ATCC BAA-332T).";
RL J. Bacteriol. 194:5120-5120(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:EIT68803.1}.
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DR EMBL; AKGD01000003; EIT68803.1; -; Genomic_DNA.
DR RefSeq; WP_007186933.1; NZ_AKGD01000003.1.
DR AlphaFoldDB; I8T4Y4; -.
DR STRING; 1172194.WQQ_39980; -.
DR PATRIC; fig|1172194.4.peg.3882; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000003704; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003704};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 266..363
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 644 AA; 70871 MW; 5F02CBB07F25C0A0 CRC64;
MLQSIRDRLS GPIVWFVIGL ICIPFAFWGV ESFRGGGSDP AVAKVGDKEI TQAEFRQGYE
QRYQQLVSLM GENFRPEMID QARFRQNVIN DMVQESLMRQ YTQAEGYRAT DAAVFDYLSS
VPAFQENGKF SAQLYRDLLA RRGMNPQTFE SQLRSSLVID QLRETIVDSA FVSSQEAALA
YRLEAQQRDV SVALFSVEKL KAAAQVTDAQ VSEHYQANKS RYTAPERLKL SYVDLDVSQL
PKAENPGADV LKTLYDAEKD SRFASPEERK ARHILVNFGA DKSEAKKKIE KFAEQIKGGA
DFATLAKENS DDTGSKAAGG DLGWVRRGVM VGKFEEALFG LKQGQVSDPV ETEFGWHLIQ
LEELKAPAIR PFEDAEVQAE LLDVYQQRDL QKRFQEKSEK LGELAFENPT SLDAVAKALD
LKVQTTDWFT REGGAGILAD DGVKQAAFST EVLTDNENSK PLPLGQERVV VIRKAEYEAP
RERKLEEVAE TIKDEIKLET AKTQVASKAD ELIKALQTGL TLQAAADAAG ASVAYTGTVK
RTDAQPDRAT LDAAFRLPRP ADGKTSTGKA VLANGDVSVV VLSKVTEPSA ADASAASSER
SRLREQVAGA EFGSMRKALE KEIKVEIKQT EVDEAATEGE GVAP
//