HPNP_RHOPT
ID HPNP_RHOPT Reviewed; 527 AA.
AC B3QHD1;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Hopanoid C-2 methylase {ECO:0000305};
DE EC=2.1.1.- {ECO:0000305};
GN Name=hpnP {ECO:0000303|PubMed:20421508};
GN OrderedLocusNames=Rpal_4269 {ECO:0000312|EMBL:ACF02765.1};
OS Rhodopseudomonas palustris (strain TIE-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=395960;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIE-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA Newman D.K., Roden E., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION IN METHYLATION OF HOPANOIDS, AND DISRUPTION PHENOTYPE.
RC STRAIN=TIE-1;
RX PubMed=20421508; DOI=10.1073/pnas.0912949107;
RA Welander P.V., Coleman M.L., Sessions A.L., Summons R.E., Newman D.K.;
RT "Identification of a methylase required for 2-methylhopanoid production and
RT implications for the interpretation of sedimentary hopanes.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:8537-8542(2010).
RN [3]
RP INDUCTION.
RC STRAIN=TIE-1;
RX PubMed=23524612; DOI=10.1128/jb.00186-13;
RA Kulkarni G., Wu C.H., Newman D.K.;
RT "The general stress response factor EcfG regulates expression of the C-2
RT hopanoid methylase HpnP in Rhodopseudomonas palustris TIE-1.";
RL J. Bacteriol. 195:2490-2498(2013).
CC -!- FUNCTION: Required for methylation of hopanoids at the C-2 position.
CC {ECO:0000269|PubMed:20421508}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q9X2H6};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000250|UniProtKB:Q9X2H6};
CC -!- INDUCTION: Up-regulated in an EcfG-dependent manner under a variety of
CC stresses, including high-temperature, acidic, alkaline and hyperosmotic
CC conditions. {ECO:0000269|PubMed:23524612}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant does not produce C-2 methylated
CC triterpenoids. {ECO:0000269|PubMed:20421508}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}.
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DR EMBL; CP001096; ACF02765.1; -; Genomic_DNA.
DR RefSeq; WP_012497138.1; NC_011004.1.
DR AlphaFoldDB; B3QHD1; -.
DR SMR; B3QHD1; -.
DR EnsemblBacteria; ACF02765; ACF02765; Rpal_4269.
DR KEGG; rpt:Rpal_4269; -.
DR HOGENOM; CLU_021572_5_0_5; -.
DR OMA; IVIWRQG; -.
DR OrthoDB; 973846at2; -.
DR BioCyc; MetaCyc:MON-17493; -.
DR BioCyc; RPAL395960:RPAL_RS21125-MON; -.
DR Proteomes; UP000001725; Chromosome.
DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.30.20; -; 1.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR025274; DUF4070.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR034530; HpnP-like.
DR InterPro; IPR007197; rSAM.
DR InterPro; IPR023404; rSAM_horseshoe.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF13282; DUF4070; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDF00303; hopanoid_C2-methyltransferase; 1.
DR SMART; SM00729; Elp3; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 1: Evidence at protein level;
KW Iron; Iron-sulfur; Metal-binding; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..527
FT /note="Hopanoid C-2 methylase"
FT /id="PRO_0000434048"
FT DOMAIN 36..148
FT /note="B12-binding"
FT /evidence="ECO:0000305"
FT DOMAIN 173..408
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 189
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9X2H6"
FT BINDING 193
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9X2H6"
FT BINDING 196
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250|UniProtKB:Q9X2H6"
SQ SEQUENCE 527 AA; 60033 MW; 30072297856A0286 CRC64;
MKAESGQTSR RILCVFPRYT KSFGTFQHSY PLMDDVAAFM PPQGLLVIAA YLPDEWSVRF
VDENIRAATA DDFAWADAVF VSGMHIQRQQ MNDICRRAHD FDLPVALGGP SVSACPDYYP
NFDYLHVGEL GDATDQLIAK LTHDVTRPKR QVVFTTEDRL DMTLFPIPAY ELAECSKYLL
GSIQYSSGCP YQCEFCDIPG LYGRNPRLKT PEQIITELDR MIECGIRGSV YFVDDNFIGN
RKAALDLLPH LVEWQKRTGF QLQLACEATL NIAKRPEILE LMREAYFCTI FVGIETPDPT
ALKAMHKDHN MMVPILEGVR TISSYGIEVV SGIILGLDTD TPETGEFLMQ FIEQSQIPLL
TINLLQALPK TPLWDRLQRE GRLVHDDNRE SNVDFLLPHD QVVAMWKDCM ARAYQPEALL
KRYDYQIAHA YATRLHPSTP QRASKANIKR GMIMLRNIIW QIGIRGDYKL AFWKFALRRL
IRGDIENLLL VMVVAHHLII YAREASRGHA NASNYSIRLR EAAVPAE
