ID A0A147KAL8_9BACI Unreviewed; 470 AA.
AC A0A147KAL8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Peptidase M48 domain-containing protein {ECO:0000259|Pfam:PF01435};
GN ORFNames=Q75_04330 {ECO:0000313|EMBL:KUP07733.1};
OS Bacillus coahuilensis p1.1.43.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP07733.1, ECO:0000313|Proteomes:UP000074108};
RN [1] {ECO:0000313|EMBL:KUP07733.1, ECO:0000313|Proteomes:UP000074108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., Souza V.,
RA Olmedo-Alvarez G.;
RT "Microevolution Analysis of Bacillus coahuilensis Unveils Differences in
RT Phosphorus Acquisition Strategies and Their Regulation.";
RL Front. Microbiol. 7:58-58(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KUP07733.1}.
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DR EMBL; LDYG01000020; KUP07733.1; -; Genomic_DNA.
DR RefSeq; WP_059350515.1; NZ_LDYG01000020.1.
DR AlphaFoldDB; A0A147KAL8; -.
DR STRING; 1150625.Q75_04330; -.
DR PATRIC; fig|1150625.3.peg.905; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000074108; 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:SF1; PROTEASE HTPX; 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; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000074108};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..153
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT DOMAIN 161..243
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REPEAT 378..410
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 411..444
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 470 AA; 53418 MW; C82C63A7B9CC6D90 CRC64;
MNQKNLVHQK EETYFIIAII VSVMAYLFLA LSVVGIIILA FILVSSFFVQ GIFIGNIRSN
GVKITQKQFP DFYKRVEELS GQMGLKRVPD VYVVESSGIL NAFATRLFGR HMVVLYSDIF
ELIKHDNEDE LTFVLAHELA HIKRNHMLKS VLLLPANFFP LLGEAYSRGC EYTCDRMAAT
YIQNSEAAAN ALTILAIGKE LYVNVDREAY IEQLEQEKSF FAWFSEKLST HPALPKRIDA
VEAFMKGTLP RRFKAPMGKI LLGLALAMAL YIASIIALTA MFYFIGKVVD EEWMAAGLGT
EMDFSYEYAL SEDPTELEEA FYYDDLDETR RLLEEGQDPA FILDSGETLM HEAIIDEDKR
MFLEEYLQFA DPETTNDYGN SLLDYAFQYG TVDTVDVLLS AGIGINDSDD YGYTPLMSAV
EYWASEEIIQ YLLENGADPT YSGEGQYTPI ELAEEYEMYD MVDLLESYVY
//
