ID Q9CJM0_PASMU Unreviewed; 626 AA.
AC Q9CJM0;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE RecName: Full=Periplasmic chaperone PpiD {ECO:0000256|ARBA:ARBA00040743};
DE AltName: Full=Periplasmic folding chaperone {ECO:0000256|ARBA:ARBA00042775};
GN OrderedLocusNames=PM1979 {ECO:0000313|EMBL:AAK04063.1};
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843 {ECO:0000313|EMBL:AAK04063.1, ECO:0000313|Proteomes:UP000000809};
RN [1] {ECO:0000313|EMBL:AAK04063.1, ECO:0000313|Proteomes:UP000000809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70 {ECO:0000313|EMBL:AAK04063.1,
RC ECO:0000313|Proteomes:UP000000809};
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK04063.1; -; Genomic_DNA.
DR RefSeq; WP_005725068.1; NC_002663.1.
DR AlphaFoldDB; Q9CJM0; -.
DR STRING; 272843.PM1979; -.
DR EnsemblBacteria; AAK04063; AAK04063; PM1979.
DR GeneID; 77207306; -.
DR KEGG; pmu:PM1979; -.
DR PATRIC; fig|272843.6.peg.2002; -.
DR HOGENOM; CLU_023843_1_1_6; -.
DR OrthoDB; 9812372at2; -.
DR Proteomes; UP000000809; Chromosome.
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; 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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000809};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 269..359
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 626 AA; 69441 MW; D0CF2A339BB9FA20 CRC64;
MLIEKLHGMT NSWVSKFLLG LIAVAFVLSG ITGYVFTRVD TSAVKINGEE ISQQTFYQRY
ESESERLRQQ LGAQFAALSG SPEFVAGLRQ SVLNNLINQE LLRQYADELK IGISDERVKQ
EIVTSQFFQQ EGKFDNALYQ RMLQLNGLTP DAYANIVREG LRLEQLQTGL AESEFIVPAQ
QAQLTELFFQ ARTVRLAPFS LDQVLEKQTI SDEEVSAYYE ANKGAFLVPE LAKVQYMTLT
RADVEKHIQV SDVEIAQYYQ DNKALYVSQG QQRLSHIQVA TEAEAKEIYQ ALQDGANFAG
LASARSLDKI SAENGGDLSW ASAGTFPKAF EEAANALQVG QFSQPVKVDD QFHIILVTER
KEPSTLPLEV VKTQIADQIR QNLVNNQYFS IEKQLAEKAF EHPEGLEKAA EVAGLTIQET
DFFSANDVPA ALNYPNVISA IFHSDISQGG VNSEPMNVGE QHAVLVRVIA NKPEGTRSLE
EAKADIISYL KRQKAEEIVL AEANQAAQRL NDNASSTLPE GVQFGSAEKW VFAENRDAAL
NNVIFAMSLT DNKPSYIASK ASNGEVVLVE LSHIEQGALS AAESELFTKQ LAQARQVALQ
NTLLQALRAK AKIEVNEKFF QQNEEQ
//
