ID   MIP_COXBU               Reviewed;         230 AA.
AC   P51752;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase Mip;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Macrophage infectivity potentiator;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
GN   Name=mip; OrderedLocusNames=CBU_0630;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 22-28.
RC   STRAIN=Nine Mile phase I;
RX   PubMed=8535514; DOI=10.1099/13500872-141-11-2861;
RA   Mo Y.-Y., Cianciotto N.P., Mallavia L.P.;
RT   "Molecular cloning of a Coxiella burnetii gene encoding a macrophage
RT   infectivity potentiator (Mip) analogue.";
RL   Microbiology 141:2861-2871(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
CC   -!- FUNCTION: May be an essential virulence factor associated with
CC       macrophage infectivity. Exhibits PPIase activity.
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: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}.
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DR   EMBL; U14170; AAA92352.1; -; Genomic_DNA.
DR   EMBL; AE016828; AAO90174.1; -; Genomic_DNA.
DR   RefSeq; NP_819660.1; NC_002971.3.
DR   RefSeq; WP_010957701.1; NC_002971.4.
DR   AlphaFoldDB; P51752; -.
DR   SMR; P51752; -.
DR   STRING; 227377.CBU_0630; -.
DR   EnsemblBacteria; AAO90174; AAO90174; CBU_0630.
DR   GeneID; 1208515; -.
DR   KEGG; cbu:CBU_0630; -.
DR   PATRIC; fig|227377.7.peg.615; -.
DR   eggNOG; COG0545; Bacteria.
DR   HOGENOM; CLU_013615_0_1_6; -.
DR   OMA; RHAKMAK; -.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isomerase; Reference proteome; Rotamase;
KW   Secreted; Signal; Virulence.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:8535514"
FT   CHAIN           22..230
FT                   /note="Peptidyl-prolyl cis-trans isomerase Mip"
FT                   /id="PRO_0000025530"
FT   DOMAIN          142..230
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   CONFLICT        167
FT                   /note="Q -> N (in Ref. 1; AAA92352)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   230 AA;  25518 MW;  5CDBAA323446FED6 CRC64;
     MKRLILPFLS VGLLLGTTAH AATPLKTEQD KLSYSMGVMT GKAFRKHDIK IDPQTFSMGL
     SDAYLGKETQ MTEAEMRQTL QQFEKQSLQK MQHKMKQTAQ QNAEKSRAFL TANKNKPGVK
     TLANGLQYKV LQAGQGQSPT LNDEVTVNYE GRLINGTVFD SSYKRGQPAT FPLKSVIKGW
     QEALTRMKPG AIWEIYVPPQ LAYGEQGAPG VIGPNEALIF KVNLISVKKK