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Database: UniProt
Entry: A0A496PHG1_9MICC
LinkDB: A0A496PHG1_9MICC
Original site: A0A496PHG1_9MICC 
ID   A0A496PHG1_9MICC        Unreviewed;      1022 AA.
AC   A0A496PHG1;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Alpha/beta fold hydrolase {ECO:0000313|EMBL:RKW69926.1};
GN   ORFNames=DWQ67_10700 {ECO:0000313|EMBL:RKW69926.1};
OS   Galactobacter caseinivorans.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Galactobacter.
OX   NCBI_TaxID=2676123 {ECO:0000313|EMBL:RKW69926.1, ECO:0000313|Proteomes:UP000273119};
RN   [1] {ECO:0000313|EMBL:RKW69926.1, ECO:0000313|Proteomes:UP000273119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JZ R-183 {ECO:0000313|EMBL:RKW69926.1,
RC   ECO:0000313|Proteomes:UP000273119};
RA   Hahne J., Isele D., Lipski A.;
RT   "Arthrobacter sp. nov., isolated from raw cow's milk with high bacterial
RT   count.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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:RKW69926.1}.
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DR   EMBL; QQXL01000006; RKW69926.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A496PHG1; -.
DR   Proteomes; UP000273119; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RKW69926.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Reference proteome {ECO:0000313|Proteomes:UP000273119};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           38..1022
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019731537"
FT   TRANSMEM        994..1014
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          986..1022
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          163..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1022 AA;  106592 MW;  F5216159232953CE CRC64;
     MSRSQHPSRV RRLLALSTTA AVASLTLALG CTVPAQATSA PVSQDSQASA PALTDQSAAL
     PGTSSTQAIA DATLELPKGA TVVSSANLSI PVTFTTTPNT PIKLKLVRVT DQSEVAGAQV
     SATAGADGKG TADVPAKSVE AGKYKIVDEG GLKQSGAITV TAPAAPGTEA SPAPSNSAPA
     TAAPSTTAPA QDKAAAEKKA AEAKKEAKKD ERADGLDKYY PQLAKDLFDK DGNGTYKVTG
     PTAGGKSAGI VPKGLGSYYS QKVDFSSANC VALGYGAYAK KYEPTLKRPL ECGYMIAPID
     SKKPSTGDVA IGVMRIKASG KSKGSVMWNP GGPGASGMTL ALVGALYQPE LAKDFDMIGF
     DPRGTGSSMP FSQCSTDEQL DLDRATNSWG KPLDAAEKEQ ADITKRFAKD CFENTGKAFG
     LNGGARNTLM KHLGTWDAVG DLDMLRSVVG DKKLSYVGYS YGTRLGYVYA QKFQASAGRL
     VLDGVVDPGD AKAAAALKSL NASSNRYQDL NGKPVPAAKA GAKAADSEVN SEEQDNIAQG
     AGFQDTFEQF AKDCAAKGPA DPAKQKTYGE LWPKLFAKDG SFEGDTQLQG TKFECALGQS
     QDPKVLSTNS AKLLQTLETG GVNEGLPTAY ERNLSFGDAR TGFFQALYSE DLWGTLNVGL
     ADLKAGADGT VMMSLADQYN DRDPQTGHYA PMLQAFTNIR CTDANNSANP APDAHLRKLA
     KLYDEAAPFQ AASQALGTPD YCQFWNFTGT LPQAEKLTKV PNVLVVSTSH DPATPYAAGP
     KLARMIDGTL LSVSGASHTS YNAEIKCVDD TVNNFLTSGV VPKDGDFGDK LKTPDTTKDD
     RGNTVTFPNL CKVKTFRDSD FVTSTTKAKA KDKVGFAVLH RDSEAKYTVS LTTGSGKGAA
     VKAVVNAQVA GMTTDNGGNH AGVFQVPAKT APGQYMVVLK DARGAFVASR PLTVQKTAVP
     SKPKPPVVHK PKPKPKPVAQ NSGENLSNTG SDSAGWIFGG AAAILVGAGA LLVARRRKGE
     QN
//
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