ID   NIFM_AZOVI              Reviewed;         292 AA.
AC   P14890;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Putative peptidyl-prolyl cis-trans isomerase NifM;
DE            Short=PPIase NifM;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase NifM;
GN   Name=nifM;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=2644218; DOI=10.1128/jb.171.2.1017-1027.1989;
RA   Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S.,
RA   Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT   "Physical and genetic map of the major nif gene cluster from Azotobacter
RT   vinelandii.";
RL   J. Bacteriol. 171:1017-1027(1989).
CC   -!- FUNCTION: Required for the activation and stabilization of the iron-
CC       component (NifH) of nitrogenase. Probable PPIase.
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   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC       {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; M20568; AAA64732.1; -; Genomic_DNA.
DR   PIR; F32055; F32055.
DR   AlphaFoldDB; P14890; -.
DR   SMR; P14890; -.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR014282; Nitrogen_fix_NifM.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR023058; PPIase_PpiC_CS.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   Pfam; PF00639; Rotamase; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   TIGRFAMs; TIGR02933; nifM_nitrog; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase; Nitrogen fixation; Rotamase.
FT   CHAIN           1..292
FT                   /note="Putative peptidyl-prolyl cis-trans isomerase NifM"
FT                   /id="PRO_0000193428"
FT   DOMAIN          148..243
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ   SEQUENCE   292 AA;  32802 MW;  42ED5181103699BF CRC64;
     MASERLADGD SRYYLLKVAH EQFGCAPGEL SEDQLQQADR IIGRQRHIED AVLRSPDAIG
     VVIPPSQLEE AWAHIASRYE SPEALQQALD AQALDAAGMR AMLARELRVE AVLDCVCAGL
     PEISDTDVSL YYFNHAEQFK VPAQHKAHIL VTINEDFPEN TREAARTRIE TILKRLRGKP
     ERFAEQAMKH SECPTAMQGG LLGEVVPGTL YPELDACLFQ MARGELSPVL ESPIGFHVLY
     CESVSPARQL TLEEILPRLR DRLQLRQRKA YQRKWLVCLL QQNATLENLA HG