ID D0MEP0_RHOM4 Unreviewed; 489 AA.
AC D0MEP0;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Right handed beta helix domain-containing protein {ECO:0000259|Pfam:PF13229};
GN OrderedLocusNames=Rmar_2390 {ECO:0000313|EMBL:ACY49268.1};
OS Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus
OS obamensis).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rhodothermaceae;
OC Rhodothermus.
OX NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY49268.1, ECO:0000313|Proteomes:UP000002221};
RN [1] {ECO:0000313|EMBL:ACY49268.1, ECO:0000313|Proteomes:UP000002221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43812 / DSM 4252 / R-10
RC {ECO:0000313|Proteomes:UP000002221};
RX PubMed=21304669; DOI=10.4056/sigs.46736;
RA Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E.,
RA Han C., Bruce D., Goodwin L., Chain P., Pitluck S., Ovchinikova G.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Detter J.C.;
RT "Complete genome sequence of Rhodothermus marinus type strain (R-10).";
RL Stand. Genomic Sci. 1:283-291(2009).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 9 family.
CC {ECO:0000256|ARBA:ARBA00038263}.
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DR EMBL; CP001807; ACY49268.1; -; Genomic_DNA.
DR RefSeq; WP_012844878.1; NC_013501.1.
DR AlphaFoldDB; D0MEP0; -.
DR STRING; 518766.Rmar_2390; -.
DR CAZy; PL9; Polysaccharide Lyase Family 9.
DR KEGG; rmr:Rmar_2390; -.
DR eggNOG; COG1523; Bacteria.
DR eggNOG; COG4733; Bacteria.
DR HOGENOM; CLU_030634_2_0_10; -.
DR OrthoDB; 9808066at2; -.
DR Proteomes; UP000002221; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR40088; PECTATE LYASE (EUROFUNG); 1.
DR PANTHER; PTHR40088:SF1; PECTATE LYASE PEL9; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR SMART; SM00710; PbH1; 6.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002221};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..489
FT /note="Right handed beta helix domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003012008"
FT DOMAIN 109..281
FT /note="Right handed beta helix"
FT /evidence="ECO:0000259|Pfam:PF13229"
SQ SEQUENCE 489 AA; 53817 MW; 3E6BFE7AAC45050C CRC64;
MKQYMLGVLL LSWAAVAYGQ RAYFVAPDGN DTTGDGSKTA PWATLNYAIA RVTAGDTIYL
RGGQYNWTSR VNINNAGTPE AYLYIWAYPG ETPVLNFEGN PDEGIRLRGW YVHLKGLVVQ
RAGDNGIRIN GSYNIIEQVV VRENGDSGLQ LDNGAAHNLI LNVDSYRNYD AANHGENADG
FAAKFGLGPG NVFRGCRAFE NSDDGFDFWE AGEGVRVEDS WSFDNGYNRW DDPSFEGDSN
GFKLGHGEGA HVLIRNLAWG HRAHGFDVNG NQTGVTLYNN TAYRNLGRNF YFDEHNSAHV
LRNNLSVEGR ELIYPEIDDA YNNWNLGILP TSDDFLSLDT TGVRGPRQPD GSLPRLDLLR
LAEGSRLIDA GIDVGLPFVG AAPDLGAYEF GLSTSVALQR PVAFRLLAPY PNPFRQAVRV
RFELASAAVV SLSVWDLTGR RVAVLLDAPQ HAGVHEVRWE PPTGLAAGLY LLVLEADGYR
ARQPLVYVR
//
