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Database: UniProt
Entry: V4PAB8_9CAUL
LinkDB: V4PAB8_9CAUL
Original site: V4PAB8_9CAUL 
ID   V4PAB8_9CAUL            Unreviewed;       506 AA.
AC   V4PAB8;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Pectate lyase superfamily protein domain-containing protein {ECO:0000259|Pfam:PF12708};
GN   ORFNames=AEAC466_09830 {ECO:0000313|EMBL:ESQ84034.1};
OS   Asticcacaulis sp. AC466.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=1282362 {ECO:0000313|EMBL:ESQ84034.1, ECO:0000313|Proteomes:UP000017826};
RN   [1] {ECO:0000313|EMBL:ESQ84034.1, ECO:0000313|Proteomes:UP000017826}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC466 {ECO:0000313|EMBL:ESQ84034.1,
RC   ECO:0000313|Proteomes:UP000017826};
RX   PubMed=24463524; DOI=10.1038/nature12900;
RA   Jiang C., Brown P.J., Ducret A., Brun Y.V.;
RT   "Sequential evolution of bacterial morphology by co-option of a
RT   developmental regulator.";
RL   Nature 506:489-493(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 28 family.
CC       {ECO:0000256|ARBA:ARBA00008834, ECO:0000256|RuleBase:RU361169}.
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:ESQ84034.1}.
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DR   EMBL; AWGE01000008; ESQ84034.1; -; Genomic_DNA.
DR   RefSeq; WP_023457975.1; NZ_AWGE01000008.1.
DR   AlphaFoldDB; V4PAB8; -.
DR   STRING; 1282362.AEAC466_09830; -.
DR   PATRIC; fig|1282362.3.peg.1941; -.
DR   eggNOG; COG5434; Bacteria.
DR   OrthoDB; 9795222at2; -.
DR   Proteomes; UP000017826; Unassembled WGS sequence.
DR   GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR000743; Glyco_hydro_28.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR024535; Pectate_lyase_SF_prot.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR31339; PECTIN LYASE-RELATED; 1.
DR   PANTHER; PTHR31339:SF70; PLASMIN AND FIBRONECTIN-BINDING PROTEIN A; 1.
DR   Pfam; PF00295; Glyco_hydro_28; 1.
DR   Pfam; PF12708; Pectate_lyase_3; 1.
DR   SMART; SM00710; PbH1; 6.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361169};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017826};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..506
FT                   /note="Pectate lyase superfamily protein domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004723501"
FT   DOMAIN          25..78
FT                   /note="Pectate lyase superfamily protein"
FT                   /evidence="ECO:0000259|Pfam:PF12708"
SQ   SEQUENCE   506 AA;  53737 MW;  B863FE1B067B3B63 CRC64;
     MIRRSLLTGA AALIALPALA ARGLFDVRDF GARGDGVTVD SPAINRAVAA AVKAGGGTVL
     LPAGRYLSFS IRLFDNITLL LAEGCVLEAA DPAIHKGGYD VAEADLPEQF QDFGITQFHC
     SLIYADGADH VSVIGRGVIH GKGLVREDPG ARWHGVTGWI APRSADPKEV AMQGKGIRAL
     GLKNCRNVLV RDITILQGGH FACHLLGCRN ATIDTILVDT DRDGIDVDCC RDVQVVNCRV
     NAPKDDAIVV KSSYALGRKI VSENISITNC RTSGFAMGSV LDGTYRASDY RSVDDIGVLG
     RIKLGTESNG GFRNIRISDC DCENTRGILV GVVDGGVLED VVISNIVLRN PVNHPLFVRQ
     AARLRAPEGT SVGACRRVRF DTIQVSGADG RYPCGVQGIP DAPIMDVSFR NVLVVSSGGG
     TAEDAARTPK EKRESSLEVS FMGTLPAYGF YARNVRGLTL TGCTFEVEKP DARPVIVLDD
     VKGGRIDGFA SNTVVQKNGS DITTVS
//
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