ID   VOLA_VIBCH              Reviewed;         796 AA.
AC   Q9KL83;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Lysophospholipase VolA;
DE   AltName: Full=Vibrio outer membrane lysophospholipase A;
DE   Flags: Precursor;
GN   Name=volA; OrderedLocusNames=VC_A0863;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, GENE NAME,
RP   AND MUTAGENESIS OF GLY-20.
RC   STRAIN=El Tor C6706 / Serotype O1;
RX   PubMed=23674613; DOI=10.1128/mbio.00305-13;
RA   Pride A.C., Herrera C.M., Guan Z., Giles D.K., Trent M.S.;
RT   "The outer surface lipoprotein VolA mediates utilization of exogenous
RT   lipids by Vibrio cholerae.";
RL   MBio 4:E305-E305(2013).
CC   -!- FUNCTION: Required for the utilization of the prevalent host lipid
CC       lysophosphatidylcholine (LPC). Functions as a lipase that cleaves
CC       exogenous LPC and generates free fatty acids, which are then
CC       transported into the cell by fatty acid transporters such as FadL, and
CC       used in various metabolic pathways. {ECO:0000269|PubMed:23674613}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane
CC       {ECO:0000269|PubMed:23674613}; Lipid-anchor {ECO:0000255|PROSITE-
CC       ProRule:PRU00303, ECO:0000269|PubMed:23674613}. Note=Surface-exposed.
CC   -!- INDUCTION: Induced in the presence of LPC.
CC       {ECO:0000269|PubMed:23674613}.
CC   -!- DISRUPTION PHENOTYPE: Mutant cannot grow with LPC as the sole carbon
CC       source. {ECO:0000269|PubMed:23674613}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
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DR   EMBL; AE003853; AAF96761.1; -; Genomic_DNA.
DR   PIR; H82406; H82406.
DR   RefSeq; NP_233249.1; NC_002506.1.
DR   RefSeq; WP_000815658.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KL83; -.
DR   STRING; 243277.VC_A0863; -.
DR   ESTHER; vibch-VCA0863; Lipase_bact_N_lipase.
DR   PRIDE; Q9KL83; -.
DR   DNASU; 2612850; -.
DR   EnsemblBacteria; AAF96761; AAF96761; VC_A0863.
DR   KEGG; vch:VC_A0863; -.
DR   PATRIC; fig|243277.26.peg.3479; -.
DR   eggNOG; COG2267; Bacteria.
DR   HOGENOM; CLU_010857_0_0_6; -.
DR   OMA; RFAKGHH; -.
DR   BioCyc; VCHO:VCA0863-MON; -.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR020009; Extracell_lipase_Pla-1/cef_e.
DR   InterPro; IPR025920; Lipase_bact_N.
DR   Pfam; PF12262; Lipase_bact_N; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR03502; lipase_Pla1_cef; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Lipid metabolism; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           19..796
FT                   /note="Lysophospholipase VolA"
FT                   /id="PRO_0000429584"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         20
FT                   /note="G->D: Does not grow with LPC as the sole carbon
FT                   source. Mislocalizes to the inner membrane."
FT                   /evidence="ECO:0000269|PubMed:23674613"
SQ   SEQUENCE   796 AA;  83562 MW;  3B1DD33E62E6D9E6 CRC64;
     MKQVIKLSLL CSALWLAGCG DETNSSGAST EVVYESYIQQ ALQRDTTIKF ALSGKDANVP
     LPSFALMNAK DGTLEIPPGS NTSGSNPLVA MGQVDGWPIT MPLFLDFKGA GLADNIITSG
     IYLYELTDSM TGSPSIKALL TNGVDYTAVS SAASDKILIM PTKALNASSE YILAVTSEVS
     DANGNPVGTS ASYAALKSKN KIYSEGDIAT LQKVTQGVEK IFQLSGVDET QIVYSTWFST
     QSVSNTLFAT RGATASAFAS GSNQLETVWK QTGLGLDTAY TIQLGTPVDF AAALTADDNF
     STYVGADKKT AILGTYTANT VDVTKGTVRL PYYLETGSNW NTQPFESAMP SLAKIKAALA
     DSKEQLTIGS QLLAAGIDTT KLATDASEQL KLMGLTLTKS DGTALDPERY ITRYSPVPKV
     KSVQDVPFLL FTPAGAAPTD IVIYQHGVTT AKENAYAFAK NLTAVGLAVI AIDLPLHGER
     SLDSTRSANS DPLAYINLTY LAVARDNLRQ SILDVLGLRA ALTLSQPLFT GTRLSGINVG
     TGSKVRMLGH SLGGIVGTSA IAESNKTLGS TAADAMYSFS GAAIQNSGGQ ISNLLLGSAF
     FGPKIKHNVA LSASTEYKGF ADAQCASLDD SACYNLFTSL ATQEQLAQVT SGFQMFSYAA
     QTLLDTIDPY SVVSTKLNNG GLTTPLYFSE VDGDSVVPNK VSNPTGSLVY LSPQFAGTEP
     LATLLGLTTV NAGQTAPNAT KSFVQFNSTA KHSTFVAPQD AGYADLAHHT EMQTETADFL
     ADDSLGAVSN SNSVLK