ID A0A0C2VQ47_9BACL Unreviewed; 426 AA.
AC A0A0C2VQ47;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN ORFNames=KR50_08980 {ECO:0000313|EMBL:KIL51017.1};
OS Jeotgalibacillus campisalis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=220754 {ECO:0000313|EMBL:KIL51017.1, ECO:0000313|Proteomes:UP000031972};
RN [1] {ECO:0000313|EMBL:KIL51017.1, ECO:0000313|Proteomes:UP000031972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-57 {ECO:0000313|EMBL:KIL51017.1,
RC ECO:0000313|Proteomes:UP000031972};
RA Goh K.M., Chan K.-G., Yaakop A.S., Ee R., Gan H.M., Chan C.S.;
RT "Jeotgalibacillus campisalis genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU003983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC -!- SIMILARITY: Belongs to the peptidase M48 family.
CC {ECO:0000256|RuleBase:RU003983}.
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:KIL51017.1}.
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DR EMBL; JXRR01000008; KIL51017.1; -; Genomic_DNA.
DR RefSeq; WP_041055334.1; NZ_JXRR01000008.1.
DR AlphaFoldDB; A0A0C2VQ47; -.
DR PATRIC; fig|220754.4.peg.918; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000031972; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07325; M48_Ste24p_like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001915; Peptidase_M48.
DR PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR PANTHER; PTHR43221:SF2; PROTEASE HTPX HOMOLOG; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01435; Peptidase_M48; 2.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU003983};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW Reference proteome {ECO:0000313|Proteomes:UP000031972};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT TRANSMEM 20..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..154
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT DOMAIN 156..240
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REPEAT 302..334
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 335..367
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 426 AA; 46533 MW; 0DAC6497CE9477DD CRC64;
MTAGPVKSER ETIYFVIGAV YSAIIYLIAI ISIIGIGIAL AVLAVVLFMN ATMLGSIRGN
GIRISHQQFG DVYERVEELS SKMGLKKTPD VFVIQSEGAL NAFATRFFGR NMVVLYSEVF
ELARQQGSAE LDFIIAHELA HIKRRHVWKN ILLMPAQLLP FLSQAYSRSC EYTCDREAAY
MTGDGEAAKR ALTILGAGKL IAREVNEDAY LEQIRSESNG AVWLSEILST HPLLPKRIQS
VGLFMNNETT PLYRPNFRKI AVGASLLFGG LFGAYIAVLL AFTVGTTVFA SLLPGEEFEE
YESASPLMDA ASYGELEIME DLIADGEDIE ETDTDGSTPL MYAVYASQND AAQLLLEEGA
DPNASDTFTS PIVLAVSNEN DELAALLYQY GADPVAEDSE GDSAYSLLNV STEEEFKEVL
GIQNSN
//
