ID Q4L7E5_STAHJ Unreviewed; 324 AA.
AC Q4L7E5;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 119.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|ARBA:ARBA00013194};
DE EC=5.2.1.8 {ECO:0000256|ARBA:ARBA00013194};
GN Name=prsA {ECO:0000313|EMBL:BAE04430.1};
GN OrderedLocusNames=SH1121 {ECO:0000313|EMBL:BAE04430.1};
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE04430.1, ECO:0000313|Proteomes:UP000000543};
RN [1] {ECO:0000313|EMBL:BAE04430.1, ECO:0000313|Proteomes:UP000000543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE04430.1,
RC ECO:0000313|Proteomes:UP000000543};
RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000971};
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DR EMBL; AP006716; BAE04430.1; -; Genomic_DNA.
DR RefSeq; WP_011275422.1; NC_007168.1.
DR AlphaFoldDB; Q4L7E5; -.
DR GeneID; 58062684; -.
DR KEGG; sha:SH1121; -.
DR eggNOG; COG0760; Bacteria.
DR HOGENOM; CLU_034646_6_2_9; -.
DR OrthoDB; 14196at2; -.
DR Proteomes; UP000000543; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|PROSITE-
KW ProRule:PRU00278}; Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..324
FT /note="peptidylprolyl isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007923862"
FT DOMAIN 139..245
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT REGION 153..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 35975 MW; F342F360191E4D03 CRC64;
MKIMNKLIVP VTASALLLGA CGSNATDSES NTLISSKAGD VKVKDVMNKI GDEQIASTSF
SIALNKILAD KYKDKVDTKD IDDEIKKEQK QYGGKDQFES MLKQQGMSLD DYKEQKKLAA
YQKQLLADKV KVSDKELKEN TKKASHILIK VKSSSSDKEG LSDKKAKEKA EKIQKEVEKN
PDKFGEIAKK ESMDSSSAKK DGSLGYVVKG QMVSKFEKAL FKLKEGQVSD VVKTDYGYHV
IKADKESDFD KQKSKLKAKL IEQKVQKDPK ILTNAYKDLL KEYDVDYKDS DIKKAVENTI
LNPEKLKQQQ SSSDSSSAAS GLSS
//
