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Database: UniProt
Entry: A8FFE6_BACP2
LinkDB: A8FFE6_BACP2
Original site: A8FFE6_BACP2 
ID   A8FFE6_BACP2            Unreviewed;       282 AA.
AC   A8FFE6;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Competence protein {ECO:0000313|EMBL:ABV62963.1};
GN   OrderedLocusNames=BPUM_2294 {ECO:0000313|EMBL:ABV62963.1};
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750 {ECO:0000313|EMBL:ABV62963.1, ECO:0000313|Proteomes:UP000001355};
RN   [1] {ECO:0000313|EMBL:ABV62963.1, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ABV62963.1,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000256|ARBA:ARBA00005525}.
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DR   EMBL; CP000813; ABV62963.1; -; Genomic_DNA.
DR   RefSeq; WP_012010642.1; NZ_VEIS01000005.1.
DR   AlphaFoldDB; A8FFE6; -.
DR   STRING; 315750.BPUM_2294; -.
DR   KEGG; bpu:BPUM_2294; -.
DR   eggNOG; COG0345; Bacteria.
DR   HOGENOM; CLU_042344_2_1_9; -.
DR   OrthoDB; 9805754at2; -.
DR   Proteomes; UP000001355; Chromosome.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:InterPro.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 1.10.3730.10; ProC C-terminal domain-like; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR028939; P5C_Rdtase_cat_N.
DR   InterPro; IPR029036; P5CR_dimer.
DR   InterPro; IPR000304; Pyrroline-COOH_reductase.
DR   PANTHER; PTHR11645:SF51; COME OPERON PROTEIN 4; 1.
DR   PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF14748; P5CR_dimer; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   3: Inferred from homology;
KW   NADP {ECO:0000256|PIRSR:PIRSR000193-1}.
FT   DOMAIN          3..93
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          162..262
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         6..11
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   282 AA;  30834 MW;  9549077EE3022853 CRC64;
     MNIGIIGTGN MGTILTEAFI ESKAVNPSSI TITNRTIEKA FNIKKNHPEL EVTKQLTGAV
     SNKDFIFVCV KPLDIYPLLK ELSPLLTEHQ TIVIITSPVH PEQIQDIVPC QTARLIPSIT
     NRALSGASLL TFGSSCSVAT KTALRQLASC ISTPIEIHHS ITRAASDIVS CGPAFISFLV
     QKMIEAAVEE TDISKEEATT LSEDMLVGLG RLIEKRLYTL PTLQDKVCVK GGVTGEGIKA
     LEAGVQDMFH RLFQNTHEKF DEDLEAVAQQ YPPSVFTDDR RN
//
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