ID K6D2K4_9BACI Unreviewed; 800 AA.
AC K6D2K4;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
GN ORFNames=BABA_14757 {ECO:0000313|EMBL:EKN66727.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN66727.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN66727.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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:EKN66727.1}.
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DR EMBL; AJLS01000114; EKN66727.1; -; Genomic_DNA.
DR RefSeq; WP_007085947.1; NZ_AJLS01000114.1.
DR AlphaFoldDB; K6D2K4; -.
DR STRING; 1117379.BABA_14757; -.
DR PATRIC; fig|1117379.3.peg.3045; -.
DR eggNOG; COG2866; Bacteria.
DR Proteomes; UP000006316; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF13290; CHB_HEX_C_1; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006316};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 249..671
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
SQ SEQUENCE 800 AA; 87600 MW; BB6FD9C0E39D1B41 CRC64;
MTKEKKQKWK RNLLVMTTVT GLGFSTFYPG LSIPAAAVEQ PDQPLPAEES VSIVQLVVPN
DNAKDKLLEL GIDLTHRIEE HDGVYEVDAV VTPSEIAMLK TFGINVKETL ITENQWNARV
EERQSAVQLQ ASLATSEDTL KVLRANHFTN QSGTFLYLEV KSSSGATAST ALKATWTENG
EEKSATLSRK VDYGEYLYHY LLLPVSAAPL SVKIESNLGG SATSSVTEWL GQEPKHPKTD
YVTDFVDHYM APNELYERAE KLAKEFPNLV DIIEMPNKTN GYRRLAQAAI GSTTNTTVVV
SSKAWGHEGG NDVSVEFRNP GTSNAPLKVT VDGKKILVDL ATDSSGKATS TAKQVVDALN
AQAGQLVTAT TYRGNAGTGV VAPTTVKLTD GLKAPADVSR DPFTVKAIRI GKHRDGSKPG
VLGYAQEHAR EWVTPLVTIE TAERLLRNYA HDSGTRKLVD NLDIFLVPTV NPDGANFSFN
DYNMQRKNMT NHCDPTASDP NYRNNWGVDL NRNHSIGSAF DGYIGASTTI CTSDTYAGPA
ENSEPEAKNL VWLADQNPNI KFAMNIHSYG GYFMWSPGAY DANRKTLPRP TAGEEAFYWA
VSDIMLNDIQ DHRGTVILPS RTGPVPDVLY SAAGNSADYL WYEKGIYAWD FEVGADLWNK
DTNRWQAVGF QPTFAEGHEE AMEFSNGLIG MIKVAYNNAK DHQPPSSKAT PGNGKYTGPV
DVKIDTSEAA TVYYTLDGSR PTFQSAKINL SGTREFAETL KIDKTTTINY FSVDAAGNIE
KNYNPLGNGK NYNSVTITIK
//
