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Database: UniProt
Entry: F7NRL5_9GAMM
LinkDB: F7NRL5_9GAMM
Original site: F7NRL5_9GAMM 
ID   F7NRL5_9GAMM            Unreviewed;       564 AA.
AC   F7NRL5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Lysophospholipase L1-like esterase {ECO:0000313|EMBL:EGM79515.1};
GN   ORFNames=Rhein_0399 {ECO:0000313|EMBL:EGM79515.1};
OS   Rheinheimera sp. A13L.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM79515.1, ECO:0000313|Proteomes:UP000004282};
RN   [1] {ECO:0000313|EMBL:EGM79515.1, ECO:0000313|Proteomes:UP000004282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A13L {ECO:0000313|EMBL:EGM79515.1,
RC   ECO:0000313|Proteomes:UP000004282};
RX   PubMed=21742876; DOI=10.1128/JB.05636-11;
RA   Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.;
RT   "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from Pangong
RT   Lake, India.";
RL   J. Bacteriol. 193:5873-5874(2011).
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000256|ARBA:ARBA00008668}.
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:EGM79515.1}.
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DR   EMBL; AFHI01000002; EGM79515.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7NRL5; -.
DR   STRING; 506534.Rhein_0399; -.
DR   eggNOG; COG2755; Bacteria.
DR   eggNOG; COG4677; Bacteria.
DR   Proteomes; UP000004282; Unassembled WGS sequence.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030599; F:pectinesterase activity; IEA:InterPro.
DR   GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR   CDD; cd01821; Rhamnogalacturan_acetylesterase_like; 1.
DR   Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR000070; Pectinesterase_cat.
DR   InterPro; IPR037459; RhgT-like.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR43695; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G17250)-RELATED; 1.
DR   PANTHER; PTHR43695:SF1; RHAMNOGALACTURONAN ACETYLESTERASE; 1.
DR   Pfam; PF00657; Lipase_GDSL; 1.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
PE   3: Inferred from homology;
KW   Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..564
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011109574"
FT   DOMAIN          30..205
FT                   /note="Pectinesterase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01095"
SQ   SEQUENCE   564 AA;  64129 MW;  F638FC6ADB5705E2 CRC64;
     MKFITAWLSA LALNLLCLNL HASEQPLRLQ VALDGSAPFN SIQQALDSLP STKEWALIEI
     GPGIYKEKLY LNRDKVVLAG SGKTSTTIEF PELRKNHLKQ QPDDWGSAVV NIKASDIVLL
     DLTVFNSYGA LYGDHDHQFA IRGFEQASRI ITDQCRVIAG GADSLSLWNK KGLYYHSNCY
     FEGHVDYVCP RGTAWIKQSQ FYSQATEASL WHDGELDQNA KLVVTDSKLS GIHGFLLGRR
     HYDAQFYLQN NQYSPLMADK PIFRKTYPDE PSRDRANLWG ERSYFSGSSG ATYGWLQNNW
     PKAVSQITED WVYQGQWQPE QLLKTIRSWL KSKAQPMPAK LYLVGDSTMS DKTNLAYPER
     GWGQLLPEFL LPQLQVINLA ANGRSTLRFL NEGRWQMLLD ELQAGDYVLI QFGHNDQKQD
     DPKRYAEVNT RYPELLQQFI REVKAKAAIP MLASSICRRN FKGKTLERDL AAYAAQAKQQ
     AELAQIDLFD LQQQSCDFWQ ELGAAGSQPY FIQVPAGLYQ KFPQGKTDNT HLSVQGASKV
     AQLFVQDLQK QHHPLARYIY RTKL
//
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