ID A0A245ZL95_9SPHN Unreviewed; 1011 AA.
AC A0A245ZL95;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Pectate lyase superfamily protein {ECO:0000313|EMBL:OWK30510.1};
GN ORFNames=SPMU_14970 {ECO:0000313|EMBL:OWK30510.1};
OS Sphingomonas mucosissima.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=370959 {ECO:0000313|EMBL:OWK30510.1, ECO:0000313|Proteomes:UP000197783};
RN [1] {ECO:0000313|EMBL:OWK30510.1, ECO:0000313|Proteomes:UP000197783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17494 {ECO:0000313|EMBL:OWK30510.1,
RC ECO:0000313|Proteomes:UP000197783};
RA Poehlein A., Wuebbeler J.H., Steinbuechel A., Daniel R.;
RT "Genome sequence of Sphingomonas mucosissima DSM 17494.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK30510.1}.
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DR EMBL; NBBJ01000002; OWK30510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A245ZL95; -.
DR OrthoDB; 7482115at2; -.
DR Proteomes; UP000197783; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR013658; SGL.
DR PANTHER; PTHR47572:SF4; LACTONASE DRP35; 1.
DR PANTHER; PTHR47572; LIPOPROTEIN-RELATED; 1.
DR Pfam; PF12708; Pectate_lyase_3; 2.
DR Pfam; PF08450; SGL; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000313|EMBL:OWK30510.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1011
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012196480"
FT DOMAIN 44..267
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
FT DOMAIN 382..432
FT /note="Pectate lyase superfamily protein"
FT /evidence="ECO:0000259|Pfam:PF12708"
FT DOMAIN 913..1000
FT /note="SMP-30/Gluconolactonase/LRE-like region"
FT /evidence="ECO:0000259|Pfam:PF08450"
SQ SEQUENCE 1011 AA; 108476 MW; BE6BF26674BA1B90 CRC64;
MIVGFLRQTA AIVMFAAATP VTAQVSAYVT APSDARAITV RGIADGRADD SAAIQQAIDA
AADRGGGGIV FLPAGSYRIT RTIYIWPGVR LFGVGEQRPR IVLGDNTPGF QRGLANMIIF
AGARRGEAEG QRVPFPPPGS VPFDRNIPDA NSGTFYSAVS NVDIAIGAGN PAATAIRFHA
AQHTFVSHMR FDLGSGLAGL YQVGNMGQDL HFRGGRYGIL AEKTSPAWPF ALIDSTFEGQ
REAAIREHEA GLTLVNVAIK DTPVGIDIDK GYGDWLWGKD VRFENVSRAA VIISNEDNVY
TQVGFENALA AGTPVFARFR DSGRTVAGKG AAYQIADFSH GLSVPTLGQM GVSKTVMEAA
PLQALPTRRP AALRSLPPTT QWHDVRQGGA KGDNSADDTA AIQRAIDTHR VVYFPAGRYV
VTDTLRLRPD SVLISLHPDL TQIVLPDGTP AFQGVGAPKA LIETARGGDA IVSGLGLFTG
GINPRATALL WMAGANSMVD DVKFQGGHGT GLADGSRFNP YNATATGDAD PAKRWDAQYP
SLWVTQGGGG TFNNIWTPNT YAQSGLYVSD TSTPGHLYQM SAEHHGRVEI ALNRVSNWEL
LAPQTEEEGG ESPDAVALEI RDSHDILVAN LHAYRVTRTK KAKPAAVTLY NSRNIRFRNV
HVNAESGLGT CDENECATFL RANKFPYENA IVDMTSGLQV REREFARLDL GDTTPPRPQP
ETIGTAAVEK LATGFDALGG ATTTPDGTLF FVDRTQQRIY RWDEKRGLGI ERDNTLDPVN
LAADRSGNLL VLSAAGRNGT VYSFRPGAPG TELTLVPAVP AQRHPSAAIA LPGNWWNNGE
FKDQLNTTTY QFTTLAQLFA SDVATAPEKV HVSPDGSLLL PAYRVFQQGP ADFRARRFSH
ALDTYGFVTA RPGTRVYVSN ASEARTYSAL VGPSGALTQL QKFAERGGES VAAEPNGRVF
IANGQIFVYD ADGRALGRID VPERPIQLLF GGADGRTLFV IGHHSIYRLR P
//
