ID A0A1M5ZVB8_9VIBR Unreviewed; 601 AA.
AC A0A1M5ZVB8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Pectate trisaccharide-lyase {ECO:0000313|EMBL:SHI28162.1};
DE EC=4.2.2.22 {ECO:0000313|EMBL:SHI28162.1};
GN Name=pelA_4 {ECO:0000313|EMBL:SHI28162.1};
GN ORFNames=VA7868_03295 {ECO:0000313|EMBL:SHI28162.1};
OS Vibrio aerogenes CECT 7868.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1216006 {ECO:0000313|EMBL:SHI28162.1, ECO:0000313|Proteomes:UP000184608};
RN [1] {ECO:0000313|EMBL:SHI28162.1, ECO:0000313|Proteomes:UP000184608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7868 {ECO:0000313|EMBL:SHI28162.1,
RC ECO:0000313|Proteomes:UP000184608};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU361173}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 1 family.
CC {ECO:0000256|RuleBase:RU361173}.
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DR EMBL; FQXZ01000037; SHI28162.1; -; Genomic_DNA.
DR RefSeq; WP_073604917.1; NZ_FQXZ01000037.1.
DR AlphaFoldDB; A0A1M5ZVB8; -.
DR STRING; 1216006.VA7868_03295; -.
DR OrthoDB; 5592990at2; -.
DR Proteomes; UP000184608; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0030570; F:pectate lyase activity; IEA:InterPro.
DR GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.290; -; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR002022; Pec_lyase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR045032; PEL.
DR PANTHER; PTHR31683; PECTATE LYASE 18-RELATED; 1.
DR PANTHER; PTHR31683:SF187; PECTATE LYASE 18-RELATED; 1.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF00544; Pectate_lyase_4; 1.
DR SMART; SM00656; Amb_all; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51173; CBM2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361173};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361173};
KW Polysaccharide degradation {ECO:0000256|RuleBase:RU361173};
KW Reference proteome {ECO:0000313|Proteomes:UP000184608};
KW Secreted {ECO:0000256|RuleBase:RU361173}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..601
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012319246"
FT DOMAIN 23..129
FT /note="CBM2"
FT /evidence="ECO:0000259|PROSITE:PS51173"
FT REGION 117..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 601 AA; 63741 MW; 126C5203A7B896C3 CRC64;
MKHVTRLLVI PATIASCYAL SIPEAAAASC SAKISDQWSN GYQMEVTINS EGNNLQNWQA
SLDFTQAPDI VNSWNAKLSV KGSLVTASNL DWNGNVPAGE STSFYIQGNG SGNAAAPSCT
LSQASSGSSQ NDTTDSSSGN ASSGNSPQAT SSGGPDGYTF CANEGESCQF SGTKKVAYGA
SGKFNYETAT NSVSCDNSTF GDPIYGSKKA CYYQQDQAPS NGPSGYTPCA KEGETCQFSG
TRKVAYGASG KFNYQLATNS ISCDNNTFGD PIYGTAKECY YGPKEDDSGN NGGGDTGSGT
CPVKLYGWAT VDGGTTGGGN VTPQRVTSLS ELRKLAKDSQ PRVLELSGTF TTGDEPIWVS
SNKTLVGIGK NTTIKGGIRI KGDKNIIIRN MSILGNNTGR PVDSIGVRGS HNIWFDHLTV
TDGPDGILDL TKGTDHVTVS WSKFYYTTKN RSHRLALLFG GGSTHGDTDT GKNNHTIHHN
WFGKNLDQRM PRLLFGKGHI YNNYYNAPGN SYAIGSGSWA SLLVENNYFK DINSPHRFQD
SNPSYITARG NIYDHTTGKK DTGAGGSGSN PPKAWTNPPY QYHLDAAKDV PSLVTSCAGP
Q
//