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Database: UniProt
Entry: Q1QXW9_CHRSD
LinkDB: Q1QXW9_CHRSD
Original site: Q1QXW9_CHRSD 
ID   Q1QXW9_CHRSD            Unreviewed;       270 AA.
AC   Q1QXW9;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=PpiC-type peptidyl-prolyl cis-trans isomerase {ECO:0000313|EMBL:ABE58689.1};
GN   OrderedLocusNames=Csal_1334 {ECO:0000313|EMBL:ABE58689.1};
OS   Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS   NCIMB 13768 / 1H11).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE58689.1, ECO:0000313|Proteomes:UP000000239};
RN   [1] {ECO:0000313|EMBL:ABE58689.1, ECO:0000313|Proteomes:UP000000239}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11
RC   {ECO:0000313|Proteomes:UP000000239};
RX   PubMed=22675587; DOI=10.4056/sigs.2285059;
RA   Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA   Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT   "Complete genome sequence of the halophilic and highly halotolerant
RT   Chromohalobacter salexigens type strain (1H11(T)).";
RL   Stand. Genomic Sci. 5:379-388(2011).
CC   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC       {ECO:0000256|ARBA:ARBA00007656}.
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DR   EMBL; CP000285; ABE58689.1; -; Genomic_DNA.
DR   RefSeq; WP_011506635.1; NC_007963.1.
DR   AlphaFoldDB; Q1QXW9; -.
DR   STRING; 290398.Csal_1334; -.
DR   KEGG; csa:Csal_1334; -.
DR   eggNOG; COG0760; Bacteria.
DR   HOGENOM; CLU_034646_9_1_6; -.
DR   OrthoDB; 9769613at2; -.
DR   Proteomes; UP000000239; Chromosome.
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; PTHR47245:SF1; FOLDASE PROTEIN PRSA; 1.
DR   PANTHER; PTHR47245; PEPTIDYLPROLYL ISOMERASE; 1.
DR   Pfam; PF00639; Rotamase; 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   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278,
KW   ECO:0000313|EMBL:ABE58689.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000239};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          112..213
FT                   /note="PpiC"
FT                   /evidence="ECO:0000259|PROSITE:PS50198"
SQ   SEQUENCE   270 AA;  29969 MW;  F8E666B232065B36 CRC64;
     MQKIAIEQIP GRASLAPVRV GEISIDEAAI ARETQYHPAE SAGDARYKAA RALVVRELLR
     QRAGQLGLAV EGESNIEVSI AALLERELEV PEPSEADCRR FHAAHAERFS EPTRLRVRHI
     LLAAAPDDAE ARDTGYRLGE TLITQLSECP ERFTEFAQRH SACPSKDKGG ELGWLAPGQT
     VPELDRALQH LATGLHARPL ASRYGWHLVS LDAREEGRAL PYDAVAERVR HSLREQATRR
     ALRHYLLALE DDIGIQGFRL DEQADGSLMQ
//
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