ID   FKBA_NEIMB              Reviewed;         272 AA.
AC   Q9JYI8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Probable FKBP-type peptidyl-prolyl cis-trans isomerase FkpA;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=fkpA; OrderedLocusNames=NMB1567;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=NZ98/254 / Serogroup B;
RX   PubMed=16645985; DOI=10.1002/pmic.200500821;
RA   Vipond C., Suker J., Jones C., Tang C., Feavers I.M., Wheeler J.X.;
RT   "Proteomic analysis of a meningococcal outer membrane vesicle vaccine
RT   prepared from the group B strain NZ98/254.";
RL   Proteomics 6:3400-3413(2006).
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- MISCELLANEOUS: Present in outer membrane vesicle formulations which are
CC       used as vaccines in human.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE002098; AAF41921.1; -; Genomic_DNA.
DR   PIR; C81068; C81068.
DR   RefSeq; NP_274574.1; NC_003112.2.
DR   RefSeq; WP_002212827.1; NC_003112.2.
DR   AlphaFoldDB; Q9JYI8; -.
DR   SMR; Q9JYI8; -.
DR   STRING; 122586.NMB1567; -.
DR   PaxDb; Q9JYI8; -.
DR   PRIDE; Q9JYI8; -.
DR   EnsemblBacteria; AAF41921; AAF41921; NMB1567.
DR   KEGG; nme:NMB1567; -.
DR   PATRIC; fig|122586.8.peg.2017; -.
DR   HOGENOM; CLU_013615_0_2_4; -.
DR   OMA; KYMSGHI; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   Gene3D; 1.10.287.460; -; 1.
DR   Gene3D; 3.10.50.40; -; 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   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF01346; FKBP_N; 1.
DR   PRINTS; PR01730; INFPOTNTIATR.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Isomerase; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Rotamase; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           21..272
FT                   /note="Probable FKBP-type peptidyl-prolyl cis-trans
FT                   isomerase FkpA"
FT                   /id="PRO_0000349891"
FT   DOMAIN          167..253
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REGION          29..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           21
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           21
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   272 AA;  28894 MW;  5BF9AD2A7A6217C8 CRC64;
     MNTIFKISAL TLSAALALSA CGKKEAAPAS ASEPAAASSA QGDTSSIGST MQQASYAMGV
     DIGRSLKQMK EQGAEIDLKV FTEAMQAVYD GKEIKMTEEQ AQEVMMKFLQ EQQAKAVEKH
     KADAKANKEK GEAFLKENAA KDGVKTTASG LQYKITKQGE GKQPTKDDIV TVEYEGRLID
     GTVFDSSKAN GGPVTFPLSQ VIPGWTEGVQ LLKEGGEATF YIPSNLAYRE QGAGDKIGPN
     ATLVFDVKLV KIGAPENAPA KQPAQVDIKK VN