ID Q5F7F3_NEIG1 Unreviewed; 272 AA.
AC Q5F7F3;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU003915};
DE EC=5.2.1.8 {ECO:0000256|RuleBase:RU003915};
GN ORFNames=NGO_1225 {ECO:0000313|EMBL:AAW89884.1};
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89884.1, ECO:0000313|Proteomes:UP000000535};
RN [1] {ECO:0000313|Proteomes:UP000000535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535};
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000256|PROSITE-
CC ProRule:PRU00277, ECO:0000256|RuleBase:RU003915};
CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC {ECO:0000256|ARBA:ARBA00006577, ECO:0000256|RuleBase:RU003915}.
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DR EMBL; AE004969; AAW89884.1; -; Genomic_DNA.
DR RefSeq; WP_003702005.1; NC_002946.2.
DR RefSeq; YP_208296.1; NC_002946.2.
DR AlphaFoldDB; Q5F7F3; -.
DR SMR; Q5F7F3; -.
DR STRING; 242231.NGO_1225; -.
DR KEGG; ngo:NGO_1225; -.
DR PATRIC; fig|242231.10.peg.1440; -.
DR HOGENOM; CLU_013615_0_1_4; -.
DR Proteomes; UP000000535; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 1.10.287.460; Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal domain; 1.
DR InterPro; IPR008104; INFPOTNTIATR.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR000774; PPIase_FKBP_N.
DR InterPro; IPR036944; PPIase_FKBP_N_sf.
DR PANTHER; PTHR43811:SF19; 39 KDA FK506-BINDING NUCLEAR PROTEIN; 1.
DR PANTHER; PTHR43811; FKBP-TYPE PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FKPA; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF01346; FKBP_N; 1.
DR PRINTS; PR01730; INFPOTNTIATR.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW ECO:0000256|RuleBase:RU003915};
KW Reference proteome {ECO:0000313|Proteomes:UP000000535};
KW Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|PROSITE-
KW ProRule:PRU00277};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..272
FT /note="Peptidyl-prolyl cis-trans isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004255511"
FT DOMAIN 167..253
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
SQ SEQUENCE 272 AA; 28922 MW; E9A285D73C7A38DA CRC64;
MNTIFKISAL TLSAALALSA CGKKEAAPAS ASEPAAASAA QGDTSSIGST MQQASYAMGV
DIGRSLKQMK EQGAEIDLKV FTDAMQAVYD GKEIKMTEEQ AQEVMMKFLQ EQQAKAVEKH
KADAKANKEK GEAFLKENAA KDGVKTTASG LQYKITKQGE GKQPTKDDIV TVEYEGRLID
GTVFDSSKAN GGPATFPLSQ VIPGWTEGVR LLKEGGEATF YIPSNLAYRE QGAGEKIGPN
ATLVFDVKLV KIGAPENAPA KQPDQVDIKK VN
//
